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1. Retracing Storage Polysaccharide Evolution in Stramenopila

Author: Malika Chabi, Marie Leleu, Léa Fermont, Matthieu Colpaert, Christophe Colleoni, Steven G. Ball, and Ugo Cenci
Subjects: laminarin, glycogen, stramenopila, metabolism, CAZy, polysaccharide, Plant culture, SB1-1110
Abstract: Eukaryotes most often synthesize storage polysaccharides in the cytosol or vacuoles in the form of either alpha (glycogen/starch)- or beta-glucosidic (chrysolaminarins and paramylon) linked glucan polymers. In both cases, the glucose can be packed either in water-soluble (glycogen and chrysolaminarins) or solid crystalline (starch and paramylon) forms with different impacts, respectively, on the osmotic pressure, the glucose accessibility, and the amounts stored. Glycogen or starch accumulation appears universal in all free-living unikonts (metazoa, fungi, amoebozoa, etc.), as well as Archaeplastida and alveolata, while other lineages offer a more complex picture featuring both alpha- and beta-glucan accumulators. We now infer the distribution of these polymers in stramenopiles through the bioinformatic detection of their suspected metabolic pathways. Detailed phylogenetic analysis of key enzymes of these pathways correlated to the phylogeny of Stramenopila enables us to retrace the evolution of storage polysaccharide metabolism in this diverse group of organisms. The possible ancestral nature of glycogen metabolism in eukaryotes and the underlying source of its replacement by beta-glucans are discussed.
Published: 2021
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2. Crystal Structures of the Catalytic Domain of Arabidopsis thaliana Starch Synthase IV, of Granule Bound Starch Synthase From CLg1 and of Granule Bound Starch Synthase I of Cyanophora paradoxa Illustrate Substrate Recognition in Starch Synthases

Author: Morten M. Nielsen, Christian Ruzanski, Katarzyna Krucewicz, Alexander Striebeck, Ugo Cenci, Steven G. Ball, Monica M. Palcic, and Jose A. Cuesta-Seijo
Subjects: starch synthase, crystal structure, SSIV, GBSS, ADP, acarbose, Plant culture, SB1-1110
Abstract: Starch synthases (SSs) are responsible for depositing the majority of glucoses in starch. Structural knowledge on these enzymes that is available from the crystal structures of rice granule bound starch synthase (GBSS) and barley SSI provides incomplete information on substrate binding and active site architecture. Here we report the crystal structures of the catalytic domains of SSIV from Arabidopsis thaliana, of GBSS from the cyanobacterium CLg1 and GBSSI from the glaucophyte Cyanophora paradoxa, with all three bound to ADP and the inhibitor acarbose. The SSIV structure illustrates in detail the modes of binding for both donor and acceptor in a plant SS. CLg1GBSS contains, in the same crystal structure, examples of molecules with and without bound acceptor, which illustrates the conformational changes induced upon acceptor binding that presumably precede catalytic activity. With structures available from several isoforms of plant and non-plant SSs, as well as the closely related bacterial glycogen synthases, we analyze, at the structural level, the common elements that define a SS, the elements that are necessary for substrate binding and singularities of the GBSS family that could underlie its processivity. While the phylogeny of the SSIII/IV/V has been recently discussed, we now further report the detailed evolutionary history of the GBSS/SSI/SSII type of SSs enlightening the origin of the GBSS enzymes used in our structural analysis.
Published: 2018
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3. Gasping for air

Author: Steven G Ball and Ugo Cenci
Subjects: symbiosis, RNA-seq, transcriptomics, endosymbiosis, Oophila amblystomatis, Ambystoma maculatum, Medicine, Science, Biology (General), QH301-705.5
Abstract: Transcriptomics is shedding new light on the relationship between photosynthetic algae and salamander eggs.
Published: 2017
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4. Sequestration of host metabolism by an intracellular pathogen

Author: Lena Gehre, Olivier Gorgette, Stéphanie Perrinet, Marie-Christine Prevost, Mathieu Ducatez, Amanda M Giebel, David E Nelson, Steven G Ball, and Agathe Subtil
Subjects: chlamydia trachomatis, host-pathogen interactions, intracellular parasites, glycogen metabolism, Medicine, Science, Biology (General), QH301-705.5
Abstract: For intracellular pathogens, residence in a vacuole provides a shelter against cytosolic host defense to the cost of limited access to nutrients. The human pathogen Chlamydia trachomatis grows in a glycogen-rich vacuole. How this large polymer accumulates there is unknown. We reveal that host glycogen stores shift to the vacuole through two pathways: bulk uptake from the cytoplasmic pool, and de novo synthesis. We provide evidence that bacterial glycogen metabolism enzymes are secreted into the vacuole lumen through type 3 secretion. Our data bring strong support to the following scenario: bacteria co-opt the host transporter SLC35D2 to import UDP-glucose into the vacuole, where it serves as substrate for de novo glycogen synthesis, through a remarkable adaptation of the bacterial glycogen synthase. Based on these findings we propose that parasitophorous vacuoles not only offer protection but also provide a microorganism-controlled metabolically active compartment essential for redirecting host resources to the pathogens.
Published: 2016
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5. Substitution of nucleotide-sugar by trehalose-dependent glycogen synthesis pathways in Chlamydiales underlines an unusual requirement for storage polysaccharides within obligate intracellular bacteria

Author: Catherine Tirtiaux, Gilbert Greub, Ugo Cenci, Derifa Kadouche, Bernadette Coddeville, Colleoni Christophe, Fabrice Bray, Loïc Couderc, Carole Kebbi-Beghdadi, Binquan Huang, Emmanuel Maes, Steven G. Ball, Hélène Touzet, Mathieu Ducatez, Trestan Pillonel, Malika Chabi, Matthieu Colpaert, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Centre de Recherche en Informatique, Signal et Automatique de Lille - UMR 9189 (CRIStAL), Centrale Lille-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Miniaturisation pour la Synthèse, l’Analyse et la Protéomique - UAR 3290 (MSAP), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Université de Lille, CNRS, Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576, Centre de Recherche en Informatique, Signal et Automatique de Lille - UMR 9189 [CRIStAL], Miniaturisation pour la Synthèse, l'Analyse et la Protéomique (MSAP) - USR 3290, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF], Miniaturisation pour la Synthèse, l’Analyse et la Protéomique - USR 3290 (MSAP), and Centre National de la Recherche Scientifique (CNRS)-Université de Lille-Institut de Chimie du CNRS (INC)
Subjects: 0303 health sciences, biology, Obligate, Glycogen, 030306 microbiology, Effector, Intracellular parasite, [SDV]Life Sciences [q-bio], biology.organism_classification, Trehalose, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, 03 medical and health sciences, Classical complement pathway, chemistry.chemical_compound, chemistry, Biochemistry, Chlamydiales, biology.protein, Glycogen synthase, 030304 developmental biology
Abstract: All obligate intracellular pathogens or symbionts of eukaryotes lack glycogen metabolism. Most members of the Chlamydiales order are exceptions to this rule as they contain the classical GlgA-GlgC-dependent pathway of glycogen metabolism that relies on the ADP-Glucose substrate. We surveyed the diversity of Chlamydiales and found glycogen metabolism to be universally present with the important exception of Criblamydiaceae and Waddliaceae families that had been previously reported to lack an active pathway. However, we now find elements of the more recently described GlgE maltose-1-P-dependent pathway in several protist-infecting Chlamydiales. In the case of Waddliaceae and Criblamydiaceae, the substitution of the classical pathway by this recently proposed GlgE pathway was essentially complete as evidenced by the loss of both GlgA and GlgC. Biochemical analysis of recombinant proteins expressed from Waddlia chondrophila and Estrella lausannensis established that both enzymes do polymerize glycogen from trehalose through the production of maltose-1-P by TreS-Mak and its incorporation into glycogen’s outer chains by GlgE. Unlike Mycobacteriaceae where GlgE-dependent polymerization is produced from both bacterial ADP-Glc and trehalose, glycogen synthesis seems to be entirely dependent on host supplied UDP-Glc and Glucose-6-P or on host supplied trehalose and maltooligosaccharides. These results are discussed in the light of a possible effector nature of these enzymes, of the chlamydial host specificity and of a possible function of glycogen in extracellular survival and infectivity of the chlamydial elementary bodies. They underline that contrarily to all other obligate intracellular bacteria, glycogen metabolism is indeed central to chlamydial replication and maintenance.
Published: 2020

6. Analysis of an improved Cyanophora paradoxa genome assembly

Author: Dana C. Price, Thamali Kariyawasam, Hwan Su Yoon, Debashish Bhattacharya, Steven G. Ball, Camilla Ferrari, Andreas P.M. Weber, Fabio Facchinelli, Jae-Hyeok Lee, Ugo Cenci, Marek Mutwil, Robyn Roth, Ursula Goodenough, Nicole E. Wagner, Cheong Xin Chan, Rutgers, The State University of New Jersey [New Brunswick] (RU), Rutgers University System (Rutgers), Washington University in Saint Louis (WUSTL), British Columbia, Nanyang Technological University [Singapour], Department of Molecular Physiology [Potsdam-Golm], Max Planck Institute of Molecular Plant Physiology (MPI-MP), Max-Planck-Gesellschaft-Max-Planck-Gesellschaft, Cluster of Excellence on Plant Sciences (CEPLAS), Universität zu Köln-Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf]-Max Planck Institute for Plant Breeding Research (MPIPZ), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), University of Queensland [Brisbane], Sungkyunkwan University [Suwon] (SKKU), School of Biological Sciences, Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf]-Max Planck Institute for Plant Breeding Research (MPIPZ)-Universität zu Köln = University of Cologne, Université de Lille-Centre National de la Recherche Scientifique (CNRS), ANR-18-CE13-0027,MATHTEST,Tester l'hypothèse du ménage à trois(2018), Université de Lille, CNRS, Rutgers, The State University of New Jersey [New Brunswick] [RU], Cluster of Excellence on Plant Sciences [CEPLAS], Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF], and Sungkyunkwan University [Suwon] [SKKU]
Subjects: Cyanophora paradoxa, Archaeplastida, phylogenomics, tree of eukaryotes, ultrastructure, 0106 biological sciences, [SDV]Life Sciences [q-bio], Peptidoglycan, Red algae, 01 natural sciences, Genome, 03 medical and health sciences, Glaucophyte, Cyanophora Paradoxa, Genetics, Glaucophyta, Viridiplantae, Molecular Biology, Phylogeny, 030304 developmental biology, 0303 health sciences, biology, Biological sciences [Science], General Medicine, Full Papers, biology.organism_classification, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, Editor's Choice, Cyanophora, Evolutionary biology, Green algae, Genome, Plant, 010606 plant biology & botany
Abstract: Glaucophyta are members of the Archaeplastida, the founding group of photosynthetic eukaryotes that also includes red algae (Rhodophyta), green algae, and plants (Viridiplantae). Here we present a high-quality assembly, built using long-read sequences, of the ca. 100 Mb nuclear genome of the model glaucophyte Cyanophora paradoxa. We also conducted a quick-freeze deep-etch electron microscopy (QFDEEM) analysis of C. paradoxa cells to investigate glaucophyte morphology in comparison to other organisms. Using the genome data, we generated a resolved 115-taxon eukaryotic tree of life that includes a well-supported, monophyletic Archaeplastida. Analysis of muroplast peptidoglycan (PG) ultrastructure using QFDEEM shows that PG is most dense at the cleavage-furrow. Analysis of the chlamydial contribution to glaucophytes and other Archaeplastida shows that these foreign sequences likely played a key role in anaerobic glycolysis in primordial algae to alleviate ATP starvation under night-time hypoxia. The robust genome assembly of C. paradoxa significantly advances knowledge about this model species and provides a reference for exploring the panoply of traits associated with the anciently diverged glaucophyte lineage.
Published: 2019

7. Biotic Host–Pathogen Interactions As Major Drivers of Plastid Endosymbiosis

Author: Agathe Subtil, Debashish Bhattacharya, Andreas P.M. Weber, Ugo Cenci, Christophe Colleoni, Steven G. Ball, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Rutgers University [Camden], Rutgers University System (Rutgers), Rheinische Friedrich-Wilhelms-Universität Bonn, Cluster of Excellence on Plant Sciences (CEPLAS), Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf]-Max Planck Institute for Plant Breeding Research (MPIPZ)-Universität zu Köln = University of Cologne, Biologie cellulaire de l'infection microbienne, Institut Pasteur [Paris] (IP), U.C., S.B., C.C., and A.S. were supported by the CNRS, the Université de Lille CNRS, the Institut Pasteur and the ANR grants ‘Expendo’ and ‘Ménage à Trois’. D.B. was supported by NSF grants MGSP 0625440 and MCB 0946528, and A.W. was supported by German Research Foundation grants CRC-TR1, CRC 1208, and EXC 1028., ANR-14-CE11-0024,Expendo,Vers l'endosymbiose expérimentale(2014), ANR-12-BSV2-0009,Ménage à trois,Une symbiose tripartite explique l'origine du plaste et son intégration métabolique(2012), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Rutgers University, Universität zu Köln-Heinrich-Heine-Universität Düsseldorf [Düsseldorf]-Max Planck Institute for Plant Breeding Research (MPIPZ), Institut Pasteur [Paris], Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Universität zu Köln-Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf]-Max Planck Institute for Plant Breeding Research (MPIPZ), and Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0301 basic medicine, Symbiogenesis, MESH: Glycogen, chlamydia, MESH: Biological Evolution, Plant Science, Biology, glycogen metabolism, Microbiology, 03 medical and health sciences, MESH: Chlamydia, evolution of plastids, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], Plastids, Plastid, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Symbiosis, Pathogen, Gene, Genetics, MESH: Symbiosis, Endosymbiosis, Obligate, Host (biology), MESH: Host-Pathogen Interactions, MESH: Plastids, biology.organism_classification, Biological Evolution, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], T3SS, bacterial conjugation, 030104 developmental biology, Host-Pathogen Interactions, Eukaryote, tryptophan synthesis, Glycogen
Abstract: International audience; The plastid originated 1.5 billion years ago through a primary endosymbiosis involving a heterotrophic eukaryote and an ancient cyanobacterium. Phylogenetic and biochemical evidence suggests that the incipient endosymbiont interacted with an obligate intracellular chlamydial pathogen that housed it in an inclusion. This aspect of the ménage-à-trois hypothesis (MATH) posits that Chlamydiales provided critical novel transporters and enzymes secreted by the pathogens in the host cytosol. This initiated the efflux of photosynthate to both the inclusion lumen and host cytosol. Here we review the experimental evidence supporting the MATH and focus on chlamydial genes that replaced existing cyanobacterial functions. The picture emerging from these studies underlines the importance of chlamydial host-pathogen interactions in the metabolic integration of the primary plastid.
Published: 2017

8. Bound Substrate in the Structure of Cyanobacterial Branching Enzyme Supports a New Mechanistic Model*

Author: Naoko Fujita, Eiji Suzuki, Mari Hayashi, Ryuichiro Suzuki, Steven G. Ball, Christophe Colleoni, CNRS, Université de Lille, Akita University, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF], Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), and Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0301 basic medicine, Models, Molecular, Glycosylation, Stereochemistry, Protein Conformation, Mutant, carbohydrate biosynthesis, cyanobacteria, enzyme mechanism, enzyme structure, glycogen, branching enzyme, starch, surface binding site, Cyanobacteria, Biochemistry, Substrate Specificity, 03 medical and health sciences, chemistry.chemical_compound, Bacterial Proteins, Protein Domains, 1,4-alpha-Glucan Branching Enzyme, Catalytic Domain, Glycogen branching enzyme, Transferase, Glycoside hydrolase, Cyanothece, Molecular Biology, Glucans, chemistry.chemical_classification, biology, Active site, Cell Biology, Enzyme structure, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, 030104 developmental biology, Enzyme, chemistry, Protein Structure and Folding, biology.protein, Mutagenesis, Site-Directed, Crystallization, Protein Binding
Abstract: Branching enzyme (BE) catalyzes the formation of α-1,6-glucosidic linkages in amylopectin and glycogen. The reaction products are variable, depending on the organism sources, and the mechanistic basis for these different outcomes is unclear. Although most cyanobacteria have only one BE isoform belonging to glycoside hydrolase family 13, Cyanothece sp. ATCC 51142 has three isoforms (BE1, BE2, and BE3) with distinct enzymatic properties, suggesting that investigations of these enzymes might provide unique insights into this system. Here, we report the crystal structure of ligand-free wild-type BE1 (residues 5–759 of 1–773) at 1.85 Å resolution. The enzyme consists of four domains, including domain N, carbohydrate-binding module family 48 (CBM48), domain A containing the catalytic site, and domain C. The central domain A displays a (β/α)8-barrel fold, whereas the other domains adopt β-sandwich folds. Domain N was found in a new location at the back of the protein, forming hydrogen bonds and hydrophobic interactions with CBM48 and domain A. Site-directed mutational analysis identified a mutant (W610N) that bound maltoheptaose with sufficient affinity to enable structure determination at 2.30 Å resolution. In this structure, maltoheptaose was bound in the active site cleft, allowing us to assign subsites −7 to −1. Moreover, seven oligosaccharide-binding sites were identified on the protein surface, and we postulated that two of these in domain A served as the entrance and exit of the donor/acceptor glucan chains, respectively. Based on these structures, we propose a substrate binding model explaining the mechanism of glycosylation/deglycosylation reactions catalyzed by BE. 292;13
Published: 2017

9. Biotic interactions as drivers of algal origin and evolution

Author: Assaf Vardi, Mahasweta Saha, Olivier De Clerck, François-Yves Bouget, Claire M. M. Gachon, J. Mark Cock, Thomas Mock, Debashish Bhattacharya, Hwan Su Yoon, Steven G. Ball, Juliet Brodie, John A. Raven, Alison G. Smith, Cheong Xin Chan, Arthur R. Grossman, The Natural History Museum [London] (NHM), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Laboratoire d'Océanographie Microbienne (LOMIC), Observatoire océanologique de Banyuls (OOB), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), University of Queensland [Brisbane], Universiteit Gent = Ghent University (UGENT), Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Station biologique de Roscoff [Roscoff] (SBR), Carnegie Institution for Science, University of East Anglia [Norwich] (UEA), University of Dundee, Helmholtz Centre for Ocean Research [Kiel] (GEOMAR), Rutgers University [Camden], Rutgers University System (Rutgers), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Universiteit Gent = Ghent University [Belgium] (UGENT), Carnegie Institution for Science [Washington], Smith, Alison [0000-0001-6511-5704], and Apollo - University of Cambridge Repository
Subjects: 0301 basic medicine, symbiome, Physiology, [SDV]Life Sciences [q-bio], Genomics, Plant Science, Biology, Phaeophyta, Algal bloom, 03 medical and health sciences, Single species, genomics, Animals, Phycodnaviridae, Ecosystem, Chromatophores, Plastids, 14. Life underwater, Photosynthesis, Symbiosis, Resilience (network), Phylogeny, trophic interactions, holobiont, Ecological niche, algae, geography, geography.geographical_feature_category, endosymbiosis, Ecology, organellogenesis, Coral reef, Eutrophication, Anthozoa, Biological Evolution, algal blooms, Holobiont, 030104 developmental biology, 13. Climate action, Host-Pathogen Interactions, Dinoflagellida
Abstract: Contents 670 I. 671 II. 671 III. 676 IV. 678 678 References 678 SUMMARY: Biotic interactions underlie life's diversity and are the lynchpin to understanding its complexity and resilience within an ecological niche. Algal biologists have embraced this paradigm, and studies building on the explosive growth in omics and cell biology methods have facilitated the in-depth analysis of nonmodel organisms and communities from a variety of ecosystems. In turn, these advances have enabled a major revision of our understanding of the origin and evolution of photosynthesis in eukaryotes, bacterial-algal interactions, control of massive algal blooms in the ocean, and the maintenance and degradation of coral reefs. Here, we review some of the most exciting developments in the field of algal biotic interactions and identify challenges for scientists in the coming years. We foresee the development of an algal knowledgebase that integrates ecosystem-wide omics data and the development of molecular tools/resources to perform functional analyses of individuals in isolation and in populations. These assets will allow us to move beyond mechanistic studies of a single species towards understanding the interactions amongst algae and other organisms in both the laboratory and the field.
Published: 2017

10. Was the Chlamydial Adaptative Strategy to Tryptophan Starvation an Early Determinant of Plastid Endosymbiosis?

Author: Steven G. Ball, Christophe Colleoni, Derifa Kadouche, Ugo Cenci, Mathieu Ducatez, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), and Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, 0301 basic medicine, Microbiology (medical), Gene Transfer, Horizontal, Immunology, Cyanobacteria, 01 natural sciences, Microbiology, trp operon, 03 medical and health sciences, Escherichia coli, Plastids, Plastid, Amino Acids, Chlamydia, Photosynthesis, Symbiosis, plastid, Gene, tryptophan metabolism, Phylogeny, 2. Zero hunger, Genetics, endosymbiosis, Chlamydiales, Endosymbiosis, biology, Archaeplastida, Effector, Tryptophan, Plants, biology.organism_classification, Biological Evolution, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, 030104 developmental biology, Infectious Diseases, Biochemistry, Host-Pathogen Interactions, Perspective, 010606 plant biology & botany
Abstract: Chlamydiales were recently proposed to have sheltered the future cyanobacterial ancestor of plastids in a common inclusion. The intracellular pathogens are thought to have donated those critical transporters that triggered the efflux of photosynthetic carbon and the consequent onset of symbiosis. Chlamydiales are also suspected to have encoded glycogen metabolism TTS (Type Three Secretion) effectors responsible for photosynthetic carbon assimilation in the eukaryotic cytosol. We now review the reasons underlying other chlamydial lateral gene transfers (LGT) evidenced in the descendants of plastid endosymbiosis. In particular, we show that half of the genes encoding enzymes of tryptophan synthesis in Archaeplastida are of chlamydial origin. Tryptophan is known to define an essential cue triggering two alternative modes of replication in Chlamydiales. In addition, sophisticated tryptophan starvation mechanisms are known to have been implemented as antibacterial defenses by their eukaryotic hosts. We propose that Chlamydiales have donated their tryptophan operon to the emerging plastid to ensure increased synthesis of tryptophan by the plastid ancestor. This would have allowed massive expression of the tryptophan rich chlamydial transporters responsible for symbiosis. It would also have allowed possible export of this valuable amino-acid in the inclusion of the tryptophan hungry pathogens. Free-living single cell cyanobacteria are devoid of proteins able to transport this amino-acid. We therefore investigated the phylogeny of the E.coli Tyr/Trp transporters and found yet another LGT from Chlamydiales to Archaeplastida thereby considerably strengthening our proposal.
Published: 2016

11. Comparison of Chain-Length Preferences and Glucan Specificities of Isoamylase-Type α-Glucan Debranching Enzymes from Rice, Cyanobacteria, and Bacteria

Author: Yoshinori Utsumi, Steven G. Ball, Kazuhiro Umeda, Taiki Kobayashi, Akiko Kubo, Christophe Colleoni, Takayuki Sawada, Naoko Fujita, Jun-ichi Abe, Satoshi Sasaki, Yasunori Nakamura, CNRS, Université de Lille, Akita University, Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576, Kagoshima University, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF], Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), and Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, 0301 basic medicine, Glycogens, Glycobiology, lcsh:Medicine, 01 natural sciences, Biochemistry, Starches, chemistry.chemical_compound, Isoamylase, lcsh:Science, Glucans, chemistry.chemical_classification, Synechococcus, Multidisciplinary, biology, Organic Compounds, Agriculture, Starch, Plants, Enzymes, Chemistry, Physical Sciences, Research Article, food.ingredient, Glycoside Hydrolases, Alpha glucan, Cyanothece, Carbohydrates, Crops, Research and Analysis Methods, Cyanobacteria, Biosynthesis, Isozyme, 03 medical and health sciences, food, Model Organisms, Polysaccharides, Plant and Algal Models, Grasses, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Glucan, Pullulanase, Bacteria, Phytoglycogen, Organic Chemistry, lcsh:R, Organisms, Chemical Compounds, Biology and Life Sciences, Proteins, Glycogen Debranching Enzyme System, Oryza, biology.organism_classification, Endosperm, 030104 developmental biology, chemistry, Enzymology, lcsh:Q, Rice, Pseudomonas amyloderamosa, 010606 plant biology & botany, Crop Science, Cereal Crops
Abstract: It has been believed that isoamylase (ISA)-type α-glucan debranching enzymes (DBEs) play crucial roles not only in α-glucan degradation but also in the biosynthesis by affecting the structure of glucans, although molecular basis on distinct roles of the individual DBEs has not fully understood. In an attempt to relate the roles of DBEs to their chain-length specificities, we analyzed the chain-length distribution of DBE enzymatic reaction products by using purified DBEs from various sources including rice, cyanobacteria, and bacteria. When DBEs were incubated with phytoglycogen, their chain-length specificities were divided into three groups. First, rice endosperm ISA3 (OsISA3) and Eschericia coli GlgX (EcoGlgX) almost exclusively debranched chains having degree of polymerization (DP) of 3 and 4. Second, OsISA1, Pseudomonas amyloderamosa ISA (PsaISA), and rice pullulanase (OsPUL) could debranch a wide range of chains of DP≧3. Third, both cyanobacteria ISAs, Cyanothece ATCC 51142 ISA (CytISA) and Synechococcus elongatus PCC7942 ISA (ScoISA), showed the intermediate chain-length preference, because they removed chains of mainly DP3-4 and DP3-6, respectively, while they could also react to chains of DP5-10 and 7–13 to some extent, respectively. In contrast, all these ISAs were reactive to various chains when incubated with amylopectin. In addition to a great variation in chain-length preferences among various ISAs, their activities greatly differed depending on a variety of glucans. Most strikingly, cyannobacteria ISAs could attack branch points of pullulan to a lesser extent although no such activity was found in OsISA1, OsISA3, EcoGlgX, and PsaISA. Thus, the present study shows the high possibility that varied chain-length specificities of ISA-type DBEs among sources and isozymes are responsible for their distinct functions in glucan metabolism. 11;6
Published: 2016

12. Pathogen to powerhouse

Author: Andreas P.M. Weber, Debashish Bhattacharya, Steven G. Ball, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Rutgers, The State University of New Jersey [New Brunswick] (RU), Rutgers University System (Rutgers), Cluster of Excellence on Plant Sciences (CEPLAS), Universität zu Köln-Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf]-Max Planck Institute for Plant Breeding Research (MPIPZ), Université de Lille-Centre National de la Recherche Scientifique (CNRS), and Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf]-Max Planck Institute for Plant Breeding Research (MPIPZ)-Universität zu Köln = University of Cologne
Subjects: 0106 biological sciences, 0301 basic medicine, Symbiogenesis, Multidisciplinary, food.ingredient, biology, fungi, Energy metabolism, biochemical phenomena, metabolism, and nutrition, biology.organism_classification, 01 natural sciences, Cell biology, Microbiology, Amoeba (genus), [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, 03 medical and health sciences, 030104 developmental biology, food, Organelle, Plastid, Paulinella, Pathogen, 010606 plant biology & botany, Archaea
Abstract: Mitochondria and plastids are essential for harnessing energy in eukaryotic cells. They are believed to have formed through primary endosymbioses, in which bacterial symbionts were converted into energy-producing organelles. Primary endosymbiosis is extremely rare: Only one other case is known, in the amoeba Paulinella ( 1 ). This rarity is usually attributed to the many innovations that are required for organelles to be integrated into the cellular machinery ( 2 ). However, the first challenges for an endosymbiont are to avoid being digested by the host and to replicate in its novel environment. Recent studies provide clues to how the precursors to mitochondria and the plastid overcame these challenges.
Published: 2016

13. Commentary: Plastid establishment did not require a chlamydial partner

Author: Andreas P.M. Weber, Steven G. Ball, Debashish Bhattacharya, Huan Qiu, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Rutgers, The State University of New Jersey [New Brunswick] (RU), Rutgers University System (Rutgers), Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf], CNRS, Université de Lille, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF], Rutgers, The State University of New Jersey [New Brunswick] [RU], and Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0301 basic medicine, Microbiology (medical), Immunology, Rickettsiales, Cyanobacteria, plastid evolution, Microbiology, Article, Glycogen debranching enzyme, mitochondria evolution, 03 medical and health sciences, Plastids, Chlamydia, Plastid, Glycogen synthase, Genetics, Chlamydiales, endosymbiosis, biology, Endosymbiosis, Phylogenetic tree, Archaeplastida, [SDV.BID.EVO]Life Sciences [q-bio]/Biodiversity/Populations and Evolution [q-bio.PE], biology.organism_classification, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, Cyanophora, 030104 developmental biology, Infectious Diseases, eukaryote evolution, Horizontal gene transfer, biology.protein, Carbohydrate Metabolism
Abstract: Primary plastids descend from the cyanobacterial endosymbiont of an ancient eukaryotic host, but the initial selective drivers that stabilized the association between these two cells are still unclear. One hypothesis that has achieved recent prominence suggests that the first role of the cyanobiont was in energy provision for a host cell whose reserves were being depleted by an intracellular chlamydial pathogen. A pivotal claim is that it was chlamydial proteins themselves that converted otherwise unusable cyanobacterial metabolites into host energy stores. We test this hypothesis by investigating the origins of the key enzymes using sophisticated phylogenetics. Here we show a mosaic origin for the relevant pathway combining genes with host, cyanobacterial or bacterial ancestry, but we detect no strong case for Chlamydiae to host transfer under the best-fitting models. Our conclusion is that there is no compelling evidence from gene trees that Chlamydiae played any role in establishing the primary plastid endosymbiosis., Primary plastids descend from an endosymbiosis involving cyanobacteria, an ancient eukaryotic host and, possibly, a chlamydial pathogen. Here, Domman and colleagues use sophisticated phylogenetic methods to show that Chlamydiae did not play a role in establishing the primary plastid endosymbiosis.
Published: 2016

14. Crystal structures of the catalytic domain of Arabidopsis thaliana Starch synthase IV, of granule bound Starch synthase from CLg1 and of granule bound Starch synthase I of Cyanophora paradoxa illustrate substrate recognition in Starch synthases

Author: Monica M. Palcic, Christian Ruzanski, Ugo Cenci, Alexander Striebeck, Jose A. Cuesta-Seijo, Steven G. Ball, Morten M. Nielsen, and Katarzyna Krucewicz
Subjects: 0301 basic medicine, ADP, crystal structure, Starch, Plant Science, lcsh:Plant culture, ternary complex, starch synthase, 03 medical and health sciences, chemistry.chemical_compound, Arabidopsis thaliana, lcsh:SB1-1110, phylogenetic tree, Ternary complex, Original Research, chemistry.chemical_classification, biology, Active site, food and beverages, Processivity, biology.organism_classification, SSIV, 030104 developmental biology, Enzyme, chemistry, Biochemistry, biology.protein, GBSS, Cyanophora paradoxa, Starch synthase, acarbose
Abstract: Starch synthases (SSs) are responsible for depositing the majority of glucoses in starch. Structural knowledge on these enzymes that is available from the crystal structures of rice granule bound starch synthase (GBSS) and barley SSI provides incomplete information on substrate binding and active site architecture. Here we report the crystal structures of the catalytic domains of SSIV from Arabidopsis thaliana, of GBSS from the cyanobacterium CLg1 and GBSSI from the glaucophyte Cyanophora paradoxa, with all three bound to ADP and the inhibitor acarbose. The SSIV structure illustrates in detail the modes of binding for both donor and acceptor in a plant SS. CLg1GBSS contains, in the same crystal structure, examples of molecules with and without bound acceptor, which illustrates the conformational changes induced upon acceptor binding that presumably precede catalytic activity. With structures available from several isoforms of plant and non-plant SSs, as well as the closely related bacterial glycogen synthases, we analyze, at the structural level, the common elements that define a SS, the elements that are necessary for substrate binding and singularities of the GBSS family that could underlie its processivity. While the phylogeny of the SSIII/IV/V has been recently discussed, we now further report the detailed evolutionary history of the GBSS/SSI/SSII type of SSs enlightening the origin of the GBSS enzymes used in our structural analysis.
Published: 2018

15. Blurred pictures from the crime scene: the growing case for a function of Chlamydiales in plastid endosymbiosis

Author: Steven G. Ball, Gilbert Greub, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Lausanne University Hospital, and Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: Plastid, Immunology, Biology, Microbiology, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, Crime scene, Plastids, Symbiosis, Chlamydiales, Endosymbiosis, Obligate, Ecology, fungi, food and beverages, Biological evolution, Plants, 16. Peace & justice, biology.organism_classification, Biological Evolution, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, Infectious Diseases, Evolutionary biology, Ménage à trois hypothesis, Function (biology), Glycogen
Abstract: A number of recent papers have brought suggestive evidence for an active role of Chlamydiales in the establishment of the plastid. Chlamydiales define a very ancient group of obligate intracellular bacterial pathogens that multiply in vesicles within eukaryotic phagotrophic host cells such as animals, amoebae or other protists, possibly including the hypothetical phagotroph that internalized the cyanobacterial ancestor of the plastid over a billion years ago. We briefly survey the case for an active role of these ancient pathogens in plastid endosymbiosis. We argue that a good understanding of the Chlamydiales infection cycle and diversity may help to shed light on the process of metabolic integration of the evolving plastid.
Published: 2015

16. Crystallization and crystallographic analysis of branching enzymes from Cyanothece sp. ATCC 51142

Author: Christophe Colleoni, Mari Hayashi, Naoko Fujita, Ryuichiro Suzuki, Eiji Suzuki, Steven G. Ball, Akita University, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), and Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: Cyanobacteria, Amino Acid Motifs, Gene Expression, medicine.disease_cause, Crystallography, X-Ray, Biochemistry, cyanobacteria, law.invention, Research Communications, Structural Biology, law, Glycoside hydrolase, amylopectin, Crystallization, Cloning, Molecular, chemistry.chemical_classification, biology, food and beverages, Condensed Matter Physics, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, glycogen, Recombinant DNA, Plasmids, food.ingredient, Cyanothece, Recombinant Fusion Proteins, Molecular Sequence Data, Biophysics, macromolecular substances, food, Bacterial Proteins, 1,4-alpha-Glucan Branching Enzyme, parasitic diseases, Genetics, Glycogen branching enzyme, medicine, Escherichia coli, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], biology.organism_classification, carbohydrates (lipids), Crystallography, Enzyme, chemistry, branching enzyme, biology.protein, bacteria, Protein Multimerization
Abstract: Several cyanobacterial species, includingCyanothecesp. ATCC 51142, remarkably have four isoforms of α-glucan branching enzymes (BEs). Based on their primary structures, they are classified into glycoside hydrolase (GH) family 13 (BE1, BE2 and BE3) or family 57 (GH57 BE). In the present study, GH13-type BEs fromCyanothecesp. ATCC 51142 (BE1, BE2 and BE3) have been overexpressed inEscherichia coliand biochemically characterized. The recombinant BE1 was crystallized by the hanging-drop vapour-diffusion method. Crystals of BE1 were obtained at 293 K in the presence of 0.2 MMg2+, 7–10%(w/v) ethanol, 0.1 MHEPES–NaOH pH 7.2–7.9. The crystals belonged to the tetragonal space groupP41212, with unit-cell parametersa = b = 133.75,c= 185.90 Å, and diffracted to beyond 1.85 Å resolution. Matthews coefficient calculations suggested that the crystals of BE1 contained two molecules in the asymmetric unit.
Published: 2015

17. Crystal Structure of the Chlamydomonas Starch Debranching Enzyme Isoamylase ISA1 Reveals Insights into the Mechanism of Branch Trimming and Complex Assembly

Author: Justin Findinier, Lyann Sim, David Dauvillée, Sophie R. Beeren, Anette Henriksen, Monica M. Palcic, Steven G. Ball, carlsberg institute, Institut carlsberg, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), CNRS, Université de Lille, IT University of Copenhagen [ITU], University of Copenhagen = Københavns Universitet [UCPH], Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF], Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF], Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Carlsberg Fondation = Carlsbergfondet [Copenhague], Université de Lille-Centre National de la Recherche Scientifique (CNRS), and Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)
Subjects: Starch, Chlamydomonas reinhardtii, Biology, Crystallography, X-Ray, Biochemistry, Glycogen debranching enzyme, chemistry.chemical_compound, Hydrolase, Glycoside hydrolase, Isoamylase, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Molecular Biology, Glucans, Protein Structure, Tertiary, Crystal Structure, X-ray Crystallography, Carbohydrate Biosynthesis, Chlamydomonas, Debranching Enzyme, Starch Metabolism, Glycosidase, Plant Proteins, Polysaccharide, food and beverages, Cell Biology, biology.organism_classification, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], chemistry, Amylopectin, Protein Structure and Folding
Abstract: International audience; The starch debranching enzymes isoamylase 1 and 2 (ISA1 and ISA2) are known to exist in a large complex and are involved in the biosynthesis and crystallization of starch. It is suggested that the function of the complex is to remove misplaced branches of growing amylopectin molecules, which would otherwise prevent the association and crystallization of adjacent linear chains. Here, we investigate the function of ISA1 and ISA2 from starch producing alga Chlamydomonas. Through complementation studies, we confirm that the STA8 locus encodes for ISA2 and sta8 mutants lack the ISA1*ISA2 heteromeric complex. However, mutants retain a functional dimeric ISA1 that is able to partly sustain starch synthesis in vivo. To better characterize ISA1, we have overexpressed and purified ISA1 from Chlamydomonas reinhardtii (CrISA1) and solved the crystal structure to 2.3 Å and in complex with maltoheptaose to 2.4 Å. Analysis of the homodimeric CrISA1 structure reveals a unique elongated structure with monomers connected end-to-end. The crystal complex reveals details about the mechanism of branch binding that explains the low activity of CrISA1 toward tightly spaced branches and reveals the presence of additional secondary surface carbohydrate binding sites.
Published: 2014

18. Progress in understanding the biosynthesis of amylose

Author: Steven G. Ball, Richard G. F. Visser, and Marion van de Wal
Subjects: chemistry.chemical_classification, Molecular mass, biology, Starch, Granule (cell biology), Plant Science, Polysaccharide, chemistry.chemical_compound, Plant Breeding, Laboratorium voor Plantenveredeling, chemistry, Biochemistry, Amylose, Amylopectin, Glycogen branching enzyme, biology.protein, Life Science, EPS, Starch synthase
Abstract: The storage of glucose in insoluble granules is a distinctive feature of plant cells. Biosynthesis of amylose, the minor low molecular mass fraction of starch occurs from ADP-glucose. This takes place within the polysaccharide matrix through the action of granule-bound starch synthase, the major protein associated with the granule. Recently, amylose has been successfully synthesized in vitro from purified granules. Two models have been proposed to explain the mechanism of amylose synthesis in plants. The first calls for priming of synthesis through small-size malto-oligosaccharides. The second suggests that glucans are extended by granule-bound starch synthase from a high molecular mass primer present within the granule. This extension is terminated through cleavage to produce amylose. This process is subsequently repeated to give several rounds of amylose synthesis.
Published: 1998

19. Convergent Evolution of Polysaccharide Debranching Defines a Common Mechanism for Starch Accumulation in Cyanobacteria and Plants

Author: Amandine Durand-Terrasson, Yasunori Nakamura, Jennifer Nirmal-Raj, Jean-Luc Putaux, Monica M. Palcic, Daiki Kobayashi, Christophe Colleoni, Lyann Sim, Emmanuel Maes, Malika Chabi, Debashish Bhattacharya, Xavier Roussel, Anne-Sophie Vercoutter-Edouart, Mathieu Ducatez, Maria Cecilia Arias, Yoshinori Utsumi, Satoshi Sasaki, Catherine Tirtiaux, Ugo Cenci, Eiji Suzuki, Steven G. Ball, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Graduate School of Agricultural and Life Sciences [UTokyo] (GSALS), The University of Tokyo (UTokyo), Centre de Recherches sur les Macromolécules Végétales (CERMAV), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), Department of Ecology, Evolution, and Natural Resources and Institute of Marine and Coastal Sciences, Rutgers University, Rutgers, The State University of New Jersey [New Brunswick] (RU), Rutgers University System (Rutgers)-Rutgers University System (Rutgers), carlsberg institute, Institut carlsberg, Université de Lille-Centre National de la Recherche Scientifique (CNRS), Université Joseph Fourier - Grenoble 1 (UJF)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Carlsberg Fondation = Carlsbergfondet [Copenhague], inconnu, Inconnu, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Department of Global Agricultural Sciences Graduate School of Agricultural and Life Sciences, The University of Tokyo, and Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)
Subjects: 0106 biological sciences, Starch, Plant Science, Biology, Photosynthesis, Polysaccharide, Cyanobacteria, 01 natural sciences, Glycogen debranching enzyme, 03 medical and health sciences, chemistry.chemical_compound, Bacterial Proteins, Plastid, Cloning, Molecular, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Phylogeny, Research Articles, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, Plant Proteins, 2. Zero hunger, chemistry.chemical_classification, 0303 health sciences, Endosymbiosis, Glycogen, food and beverages, Glycogen Debranching Enzyme System, Oryza, Cell Biology, Biological Evolution, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Enzyme, chemistry, Biochemistry, Mutagenesis, 010606 plant biology & botany
Abstract: International audience; : Starch, unlike hydrosoluble glycogen particles, aggregates into insoluble, semicrystalline granules. In photosynthetic eukaryotes, the transition to starch accumulation occurred after plastid endosymbiosis from a preexisting cytosolic host glycogen metabolism network. This involved the recruitment of a debranching enzyme of chlamydial pathogen origin. The latter is thought to be responsible for removing misplaced branches that would otherwise yield a water-soluble polysaccharide. We now report the implication of starch debranching enzyme in the aggregation of semicrystalline granules of single-cell cyanobacteria that accumulate both glycogen and starch-like polymers. We show that an enzyme of analogous nature to the plant debranching enzyme but of a different bacterial origin was recruited for the same purpose in these organisms. Remarkably, both the plant and cyanobacterial enzymes have evolved through convergent evolution, showing novel yet identical substrate specificities from a preexisting enzyme that originally displayed the much narrower substrate preferences required for glycogen catabolism.
Published: 2013

20. Chlamydia, cyanobiont, or host: who was on top in the ménage à trois?

Author: Fabio Facchinelli, Steven G. Ball, Christophe Colleoni, Andreas P.M. Weber, Institute for Plant Biochemistry, Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf], Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Heinrich-Heine-Universität Düsseldorf [Düsseldorf], Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), and Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, Glaucophyta, Plant Science, Red algae, Cyanobacteria, 01 natural sciences, 03 medical and health sciences, Botany, Plastids, Plastid, Chlamydia, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Symbiosis, 030304 developmental biology, 0303 health sciences, Endosymbiosis, biology, Obligate, Host (biology), Archaeplastida, biology.organism_classification, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Cell biology, Rhodophyta, Cyanobiont, Eukaryote, Glycogen, 010606 plant biology & botany
Abstract: International audience; : The endosymbiont hypothesis proposes that photosynthate from the cyanobiont was exported to the cytosol of the eukaryote host and polymerized from ADP-glucose into glycogen. Chlamydia-like pathogens are the second major source of foreign genes in Archaeplastida, suggesting that these obligate intracellular pathogens had a significant role during the establishment of endosymbiosis, likely through facilitating the metabolic integration between the endosymbiont and the eukaryotic host. In this opinion article, we propose that a hexose phosphate transporter of chlamydial origin was the first transporter responsible for exporting photosynthate out of the cyanobiont. This connection pre-dates the recruitment of the host-derived carbon translocators on the plastid inner membranes of green and red algae, land plants, and photosynthetic organisms of higher order endosymbiotic origin.
Published: 2013

21. Transition from glycogen to starch metabolism in Archaeplastida

Author: Christophe Colleoni, Felix Nitschke, Berge A. Minassian, Steven G. Ball, Ugo Cenci, Martin Steup, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Plant Physiology, Institute of Biochemistry and Biology, University of Potsdam, Institute of Medical Sciences, University of Toronto, Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Université de Lille-Centre National de la Recherche Scientifique (CNRS), and University of Potsdam = Universität Potsdam
Subjects: 0106 biological sciences, Starch, Chlamydiae, Plant Science, Polysaccharide, 01 natural sciences, 03 medical and health sciences, chemistry.chemical_compound, Polysaccharides, Plastids, Chlamydia, Phosphorylation, Plastid, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Phylogeny, Plant Proteins, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, biology, Glycogen, Endosymbiosis, Archaeplastida, Plants, biology.organism_classification, Biological Evolution, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Cytosol, Biochemistry, chemistry, 010606 plant biology & botany
Abstract: International audience; : In this opinion article we propose a scenario detailing how two crucial components have evolved simultaneously to ensure the transition of glycogen to starch in the cytosol of the Archaeplastida last common ancestor: (i) the recruitment of an enzyme from intracellular Chlamydiae pathogens to facilitate crystallization of α-glucan chains; and (ii) the evolution of novel types of polysaccharide (de)phosphorylating enzymes from preexisting glycogen (de)phosphorylation host pathways to allow the turnover of such crystals. We speculate that the transition to starch benefitted Archaeplastida in three ways: more carbon could be packed into osmotically inert material; the host could resume control of carbon assimilation from the chlamydial pathogen that triggered plastid endosymbiosis; and cyanobacterial photosynthate export could be integrated in the emerging Archaeplastida.
Published: 2013

22. Genome structure and metabolic features in the red seaweed Chondrus crispus shed light on evolution of the Archaeplastida

Author: Tristan Barbeyron, Wilfrid Carré, Michael Katinka, Loraine Brillet, Klaus Valentin, Karine Labadie, Betina M. Porcel, Zofia Nehr, Francisco Cabello-Hurtado, Mirjam Czjzek, Benjamin Noel, Philippe Deschamps, Susana M. Coelho, John H. F. Bothwell, Pascal J. Lopez, Marek Eliáš, François Artiguenave, François-Yves Bouget, Thierry Tonon, Jean Weissenbach, Christophe Colleoni, Deirdre H. McLachlan, Ahmed A. Moustafa, Cécile Hervé, Olivier Panaud, Catherine Boyen, Jonas Collén, Antonios Zambounis, Frédéric Partensky, Cristian Chaparro, Ludovic Delage, Jose Fernandes Barbosa-Neto, Salvador Capella-Gutierrez, Bernard Kloareg, Nathalie Kowalczyk, Gaelle Samson, Gurvan Michel, Simon M. Dittami, Jean-Marc Aury, J. Mark Cock, Patrick Wincker, Agnès Groisillier, Pi Nyvall Collén, Bénédicte Charrier, Corinne Da Silva, Catherine Leblanc, Lionel Cladière, Alok Arun, Laurence Meslet-Cladiere, Claire M. M. Gachon, Sylvie Rousvoal, Kamel Jabbari, Stefan A. Rensing, Toni Gabaldón, Steven G. Ball, Aikaterini Symeonidi, Julie Poulain, Végétaux marins et biomolécules, Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-GOEMAR-Centre National de la Recherche Scientifique (CNRS), Procaryotes Phototrophes Marins = MArine Phototrophic Prokaryotes (MAPP), Adaptation et diversité en milieu marin (AD2M), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Commissariat à l'Energie Atomique, Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Génomique métabolique (UMR 8030), Genoscope - Centre national de séquençage [Evry] (GENOSCOPE), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Laboratoire Génome et développement des plantes (LGDP), Université de Perpignan Via Domitia (UPVD)-Centre National de la Recherche Scientifique (CNRS), Alfred-Wegener-Institut, Helmholtz-Zentrum für Polar- und Meeresforschung (AWI), Department of Plant Physiology, Faculty of Sciences, Charles University [Prague] (CU), Belfast e-Science Centre [Belfast] (BESC), Queen's University [Belfast] (QUB), Laboratoire d'Océanographie Microbienne (LOMIC), Observatoire océanologique de Banyuls (OOB), Ecosystèmes, biodiversité, évolution [Rennes] (ECOBIO), Université de Rennes (UR)-Institut Ecologie et Environnement (INEE), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Observatoire des Sciences de l'Univers de Rennes (OSUR), Université de Rennes (UR)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Rennes 2 (UR2)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Rennes 2 (UR2)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Centre National de la Recherche Scientifique (CNRS), Universitat Pompeu Fabra [Barcelona] (UPF), Center for Genomic Regulation (CRG-UPF), CIBER de Epidemiología y Salud Pública (CIBERESP), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Bioinformatics and Genomics Programme, Centre for Genomic Regulation (CRG), Scottish Association for Marine Science (SAMS), Institut de biologie de l'ENS Paris (IBENS), Département de Biologie - ENS Paris, École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Biologie des Organismes et Ecosystèmes Aquatiques (BOREA), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-Muséum national d'Histoire naturelle (MNHN)-Institut de Recherche pour le Développement (IRD)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Université des Antilles (UA), Laboratoire des Sciences de l'Environnement Marin (LEMAR) (LEMAR), Institut de Recherche pour le Développement (IRD)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Université de Brest (UBO)-Institut Universitaire Européen de la Mer (IUEM), Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Department of Biology and Biotechnology Graduate Program, American University in Cairo, American University in Cairo, University of Freiburg [Freiburg], Freiburg Initiative in Systems Biology, Centre for Research and Technology Hellas (CERTH), Institut de Génomique d'Evry (IG), Université Paris-Saclay-Institut de Biologie François JACOB (JACOB), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), MArine Phototrophic Prokaryotes (MAPP), Adaptation et diversité en milieu marin (ADMM), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université d'Évry-Val-d'Essonne (UEVE), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Charles University [Prague], Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut Ecologie et Environnement (INEE), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Observatoire des Sciences de l'Univers de Rennes (OSUR)-Centre National de la Recherche Scientifique (CNRS), Universitat Pompeu Fabra [Barcelona], Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Station biologique de Roscoff [Roscoff] (SBR), Institut de biologie de l'ENS Paris (UMR 8197/1024) (IBENS), École normale supérieure - Paris (ENS Paris)-École normale supérieure - Paris (ENS Paris)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Sorbonne Université (SU)-Université des Antilles (UA)-Muséum national d'Histoire naturelle (MNHN)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut de Recherche pour le Développement (IRD), Institut de Recherche pour le Développement (IRD)-Institut Universitaire Européen de la Mer (IUEM), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Université de Brest (UBO)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS), Center for Research and Technology Hellas, Institut de Biologie François JACOB (JACOB), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Observatoire des Sciences de l'Univers de Rennes (OSUR)-Institut Ecologie et Environnement (INEE), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Département de Biologie - ENS Paris, École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS)-Université des Antilles (UA)-Muséum national d'Histoire naturelle (MNHN)-Institut de Recherche pour le Développement (IRD)-Sorbonne Université (SU)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU), Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Université d'Évry-Val-d'Essonne (UEVE), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Observatoire océanologique de Banyuls (OOB), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS Paris), Institut Universitaire Européen de la Mer (IUEM), Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Centre National de la Recherche Scientifique (CNRS)-Université de Brest (UBO), and Institut de Recherche pour le Développement (IRD)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, Transposable element, Genome evolution, [SDV]Life Sciences [q-bio], Molecular Sequence Data, Bacterial genome size, Biology, Chondrus, MESH: Base Sequence, MESH: RNA, Plant, Genes, Plant, 01 natural sciences, Genome, Evolution, Molecular, 03 medical and health sciences, MESH: Genes, Plant, 14. Life underwater, Gene, Genome size, MESH: Evolution, Molecular, 030304 developmental biology, Plant Proteins, Genetics, 0303 health sciences, Multidisciplinary, MESH: Molecular Sequence Data, Base Sequence, MESH: Plant Proteins, Archaeplastida, Biological Sciences, biology.organism_classification, MicroRNAs, RNA, Plant, MESH: MicroRNAs, MESH: Chondrus, 010606 plant biology & botany
Abstract: Red seaweeds are key components of coastal ecosystems and are economically important as food and as a source of gelling agents, but their genes and genomes have received little attention. Here we report the sequencing of the 105-Mbp genome of the florideophyte Chondrus crispus (Irish moss) and the annotation of the 9,606 genes. The genome features an unusual structure characterized by gene-dense regions surrounded by repeat-rich regions dominated by transposable elements. Despite its fairly large size, this genome shows features typical of compact genomes, e.g., on average only 0.3 introns per gene, short introns, low median distance between genes, small gene families, and no indication of large-scale genome duplication. The genome also gives insights into the metabolism of marine red algae and adaptations to the marine environment, including genes related to halogen metabolism, oxylipins, and multicellularity (microRNA processing and transcription factors). Particularly interesting are features related to carbohydrate metabolism, which include a minimalistic gene set for starch biosynthesis, the presence of cellulose synthases acquired before the primary endosymbiosis showing the polyphyly of cellulose synthesis in Archaeplastida, and cellulases absent in terrestrial plants as well as the occurrence of a mannosylglycerate synthase potentially originating from a marine bacterium. To explain the observations on genome structure and gene content, we propose an evolutionary scenario involving an ancestral red alga that was driven by early ecological forces to lose genes, introns, and intergenetic DNA; this loss was followed by an expansion of genome size as a consequence of activity of transposable elements.
Published: 2013

23. Metabolic Effectors Secreted by Bacterial Pathogens: Essential Facilitators of Plastid Endosymbiosis?

Author: Ugo Cenci, Maria Cecilia Arias, Andreas P.M. Weber, Christophe Colleoni, Lena Gehre, David Dauvillée, Debashish Bhattacharya, Ahmed A. Moustafa, Steven G. Ball, Agathe Subtil, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Biologie des Interactions Cellulaires (BIC), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Department of Ecology, Evolution, and Natural Resources and Institute of Marine and Coastal Sciences, Rutgers University, Rutgers, The State University of New Jersey [New Brunswick] (RU), Rutgers University System (Rutgers)-Rutgers University System (Rutgers), Department of Biology and Biotechnology Graduate Program, American University in Cairo, American University in Cairo, Institute for Plant Biochemistry, Heinrich-Heine-Universität Düsseldorf [Düsseldorf], Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Biologie des Interactions Cellulaires, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf], Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), and Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris]
Subjects: 0106 biological sciences, Plant Science, Cyanobacteria, 01 natural sciences, 03 medical and health sciences, Bacterial Proteins, Symbiosis, Botany, Secretion, Plastids, Photosynthesis, Plastid, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Phylogeny, Plant Proteins, 030304 developmental biology, Genetics, 0303 health sciences, Chlamydiales, biology, Endosymbiosis, Archaeplastida, Effector, fungi, Computational Biology, food and beverages, Cell Biology, Plants, biology.organism_classification, Biological Evolution, Carbon, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Host-Pathogen Interactions, Perspective, Cyanobiont, Eukaryote, Isoamylase, Genome, Plant, Glycogen, 010606 plant biology & botany
Abstract: Under the endosymbiont hypothesis, over a billion years ago a heterotrophic eukaryote entered into a symbiotic relationship with a cyanobacterium (the cyanobiont). This partnership culminated in the plastid that has spread to forms as diverse as plants and diatoms. However, why primary plastid acquisition has not been repeated multiple times remains unclear. Here, we report a possible answer to this question by showing that primary plastid endosymbiosis was likely to have been primed by the secretion in the host cytosol of effector proteins from intracellular Chlamydiales pathogens. We provide evidence suggesting that the cyanobiont might have rescued its afflicted host by feeding photosynthetic carbon into a chlamydia-controlled assimilation pathway.
Published: 2013

24. Genome of the red alga Porphyridium purpureum

Author: Steven G. Ball, Andreas P.M. Weber, Simone Zäuner, Hwan Su Yoon, Nicholas Rose, Cheong Xin Chan, Huan Qiu, Bernard Henrissat, Maria Cecilia Arias, Anagha Krishnan, Debashish Bhattacharya, Andrea Egizi, Shannon U. Morath, Marie-Mathilde Perrineau, Pedro M. Coutinho, Frédérique Hilliou, Dana C. Price, Rutgers University [Camden], Rutgers University System (Rutgers), University of Queensland [Brisbane], Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf], Architecture et fonction des macromolécules biologiques (AFMB), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Rheinische Friedrich-Wilhelms-Universität Bonn, Department of Plant Biology and Pathology, Rutgers, The State University of New Jersey [New Brunswick] (RU), Rutgers University System (Rutgers)-Rutgers University System (Rutgers), Institut Sophia Agrobiotech (ISA), Institut National de la Recherche Agronomique (INRA)-Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS), Sung Kyun Kwan University, National Science Foundation (0936884 and 1317114), Department of Defense (DoD) through the National Defense Science and Engineering Graduate (NDSEG) program, Next-Generation BioGreen 21 Program (SSAC, 2013-PJ009525), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), and COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Recherche Agronomique (INRA)
Subjects: 0106 biological sciences, plastendosymbiosis, polypeptide, [SDV]Life Sciences [q-bio], Light-Harvesting Protein Complexes, General Physics and Astronomy, 01 natural sciences, Genome, Cytochrome P-450 Enzyme System, gene transfer, Phylogeny, Genetics, 0303 health sciences, Multidisciplinary, biology, Reproduction, Starch, phycobilisome, Meiosis, Horizontal gene transfer, [SDE]Environmental Sciences, Carbohydrate Metabolism, Gene Transfer, Horizontal, General Biochemistry, Genetics and Molecular Biology, Article, cyanidioschyzon merolae, 03 medical and health sciences, cruentum, Phylogenetics, Botany, evolution, Cyanidiophyceae, Gene, 030304 developmental biology, Whole genome sequencing, Sphingolipids, meiotic genes, Algal Proteins, Intron, Membrane Transport Proteins, General Chemistry, sequence, biology.organism_classification, Sexual reproduction, Molecular Weight, Gene Ontology, Glycolipids, Porphyridium, biosynthesis, 010606 plant biology & botany
Abstract: The limited knowledge we have about red algal genomes comes from the highly specialized extremophiles, Cyanidiophyceae. Here, we describe the first genome sequence from a mesophilic, unicellular red alga, Porphyridium purpureum. The 8,355 predicted genes in P. purpureum, hundreds of which are likely to be implicated in a history of horizontal gene transfer, reside in a genome of 19.7 Mbp with 235 spliceosomal introns. Analysis of light-harvesting complex proteins reveals a nuclear-encoded phycobiliprotein in the alga. We uncover a complex set of carbohydrate-active enzymes, identify the genes required for the methylerythritol phosphate pathway of isoprenoid biosynthesis, and find evidence of sexual reproduction. Analysis of the compact, function-rich genome of P. purpureum suggests that ancestral lineages of red algae acted as mediators of horizontal gene transfer between prokaryotes and photosynthetic eukaryotes, thereby significantly enriching genomes across the tree of photosynthetic life., Red algae form one of the most ancient eukaryotic lineages, and have undergone multiple symbioses. Here, Price et al. report the first genome sequence for a mesophilic red alga, and reveal significant differences between these organisms and hyperthermopilic algae.
Published: 2013

25. A Forward Genetic Approach in Chlamydomonas reinhardtii as a Strategy for Exploring Starch Catabolism

Author: Thierry Duchêne, Justin Findinier, David Dauvillée, Charlotte Cousin, Hande Tunçay, Gilles Peltier, Virginie Cogez, Steven G. Ball, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Environnement, Bioénergie, Microalgues et Plantes (EBMP), Institut de Biosciences et Biotechnologies d'Aix-Marseille (ex-IBEB) (BIAM), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Centre National de la Recherche Scientifique (CNRS), Universite des Sciences et Technologies de Lille (USTL), Institut Francais des Materiaux Agro-Sources (IFMAS), Ministere de la recherche et de l'enseignement superieur, Region Nord Pas de Calais and the Universite des Sciences et technologies de Lille, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Bioénergie et Microalgues (EBM), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), CNRS, Université de Lille, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF], Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF], and Environnement, Bioénergie, Microalgues et Plantes [EBMP]
Subjects: 0106 biological sciences, Starch, Science, Mutant, Chlamydomonas reinhardtii, medicine.disease_cause, 01 natural sciences, Polymerase Chain Reaction, 03 medical and health sciences, chemistry.chemical_compound, medicine, Glycogen branching enzyme, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Gene, 030304 developmental biology, DNA Primers, 0303 health sciences, Mutation, Multidisciplinary, biology, Base Sequence, Maltose, biology.organism_classification, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], MESH: Starches , Polysaccharides , Iodine , Catabolism , Polymerase chain reaction , Phenotypes , Algae , Elution, chemistry, Biochemistry, biology.protein, Medicine, Green algae, 010606 plant biology & botany, Research Article
Abstract: International audience; A screen was recently developed to study the mobilization of starch in the unicellular green alga Chlamydomonas reinhardtii. This screen relies on starch synthesis accumulation during nitrogen starvation followed by the supply of nitrogen and the switch to darkness. Hence multiple regulatory networks including those of nutrient starvation, cell cycle control and light to dark transitions are likely to impact the recovery of mutant candidates. In this paper we monitor the specificity of this mutant screen by characterizing the nature of the genes disrupted in the selected mutants. We show that one third of the mutants consisted of strains mutated in genes previously reported to be of paramount importance in starch catabolism such as those encoding β-amylases, the maltose export protein, and branching enzyme I. The other mutants were defective for previously uncharacterized functions some of which are likely to define novel proteins affecting starch mobilization in green algae.
Published: 2013

26. Eukaryote to gut bacteria transfer of a glycoside hydrolase gene essential for starch breakdown in plants

Author: Steven G. Ball, Maria Cecilia Arias, Pedro M. Coutinho, Bernard Henrissat, Etienne Danchin, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), UMR 1355 ISA, Institut National de la Recherche Agronomique (INRA), Architecture et fonction des macromolécules biologiques (AFMB), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), and Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)
Subjects: Genetics, biology, gut microbiota, Prokaryote, Bacterial genome size, Gut flora, biology.organism_classification, Biochemistry, Genome, Bacterial cell structure, Bacteroides sp, Microbiology, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], DPE2, eukaryote-to-prokaryote LGT, Horizontal gene transfer, GH77, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Gene, Bacteria, Research Paper
Abstract: International audience; Lateral gene transfer (LGT) between bacteria constitutes a strong force in prokaryote evolution, transforming the hierarchical tree of life into a network of relationships between species. In contrast, only a few cases of LGT from eukaryotes to prokaryotes have been reported so far. The distal animal intestine is predominantly a bacterial ecosystem, supplying the host with energy from dietary polysaccharides through carbohydrate-active enzymes absent from its genome. It has been suggested that LGT is particularly important for the human microbiota evolution. Here we show evidence for the first eukaryotic gene identified in multiple gut bacterial genomes. We found in the genome sequence of several gut bacteria, a typically eukaryotic glycoside-hydrolase necessary for starch breakdown in plants. The distribution of this gene is patchy in gut bacteria with presence otherwise detected only in a few environmental bacteria. We speculate that the transfer of this gene to gut bacteria occurred by a sequence of two key LGT events; first, an original eukaryotic gene was transferred probably from Archaeplastida to environmental bacteria specialized in plant polysaccharides degradation and second, the gene was transferred from the environmental bacteria to gut microbes.
Published: 2012

27. The evolution of glycogen and starch metabolism in eukaryotes gives molecular clues to understand the establishment of plastid endosymbiosis

Author: Steven G. Ball, Jenifer Nirmal Raj, Catherine Tirtiaux, Christophe Colleoni, Ugo Cenci, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), and Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)
Subjects: 0106 biological sciences, Cyanobacteria, Chloroplasts, Physiology, Plant Science, 01 natural sciences, Evolution, Molecular, 03 medical and health sciences, Gene Duplication, Botany, Glaucophyta, Plastids, Plastid, Photosynthesis, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Symbiosis, 030304 developmental biology, 0303 health sciences, biology, Endosymbiosis, Archaeplastida, food and beverages, Starch, Plants, biology.organism_classification, Carbon, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Chloroplast, Biochemistry, Green algae, Eukaryote, Glycogen, 010606 plant biology & botany
Abstract: International audience; Solid semi-crystalline starch and hydrosoluble glycogen define two distinct physical states of the same type of storage polysaccharide. Appearance of semi-crystalline storage polysaccharides appears linked to the requirement of unicellular diazotrophic cyanobacteria to fuel nitrogenase and protect it from oxygen through respiration of vast amounts of stored carbon. Starch metabolism itself resulted from the merging of the bacterial and eukaryote pathways of storage polysaccharide metabolism after endosymbiosis of the plastid. This generated the three Archaeplastida lineages: the green algae and land plants (Chloroplastida), the red algae (Rhodophyceae), and the glaucophytes (Glaucophyta). Reconstruction of starch metabolism in the common ancestor of Archaeplastida suggests that polysaccharide synthesis was ancestrally cytosolic. In addition, the synthesis of cytosolic starch from the ADP-glucose exported from the cyanobacterial symbiont possibly defined the original metabolic flux by which the cyanobiont provided photosynthate to its host. Additional evidence supporting this scenario include the monophyletic origin of the major carbon translocators of the inner membrane of eukaryote plastids which are sisters to nucleotide-sugar transporters of the eukaryote endomembrane system. It also includes the extent of enzyme subfunctionalization that came as a consequence of the rewiring of this pathway to the chloroplasts in the green algae. Recent evidence suggests that, at the time of endosymbiosis, obligate intracellular energy parasites related to extant Chlamydia have donated important genes to the ancestral starch metabolism network.
Published: 2011

28. Microarray data can predict diurnal changes of starch content in the picoalga Ostreococcus

Author: François-Yves Bouget, Oksana Sorokina, Florence Corellou, Andrew J. Millar, David Dauvillée, Steven G. Ball, Igor Goryanin, Anatoly Sorokin, School of Biological science, University of Edinburgh, Laboratoire d'Océanographie Microbienne (LOMIC), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Observatoire océanologique de Banyuls (OOB), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Observatoire océanologique de Banyuls (OOB), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), and Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, Carbohydrate metabolism, 01 natural sciences, Models, Biological, Gene Expression Regulation, Enzymologic, Ostreococcus, Transcriptome, 03 medical and health sciences, Chlorophyta, Structural Biology, Modelling and Simulation, Transcriptional regulation, Gene Regulatory Networks, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Molecular Biology, lcsh:QH301-705.5, 030304 developmental biology, Genetics, Regulation of gene expression, 0303 health sciences, biology, Microarray analysis techniques, Gene Expression Profiling, Applied Mathematics, fungi, RNA, Starch, biology.organism_classification, Microarray Analysis, Computer Science Applications, Circadian Rhythm, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Gene expression profiling, Biochemistry, lcsh:Biology (General), Modeling and Simulation, Gene Deletion, Research Article, 010606 plant biology & botany
Abstract: Background The storage of photosynthetic carbohydrate products such as starch is subject to complex regulation, effected at both transcriptional and post-translational levels. The relevant genes in plants show pronounced daily regulation. Their temporal RNA expression profiles, however, do not predict the dynamics of metabolite levels, due to the divergence of enzyme activity from the RNA profiles. Unicellular phytoplankton retains the complexity of plant carbohydrate metabolism, and recent transcriptomic profiling suggests a major input of transcriptional regulation. Results We used a quasi-steady-state, constraint-based modelling approach to infer the dynamics of starch content during the 12 h light/12 h dark cycle in the model alga Ostreococcus tauri. Measured RNA expression datasets from microarray analysis were integrated with a detailed stoichiometric reconstruction of starch metabolism in O. tauri in order to predict the optimal flux distribution and the dynamics of the starch content in the light/dark cycle. The predicted starch profile was validated by experimental data over the 24 h cycle. The main genetic regulatory targets within the pathway were predicted by in silico analysis. Conclusions A single-reaction description of starch production is not able to account for the observed variability of diurnal activity profiles of starch-related enzymes. We developed a detailed reaction model of starch metabolism, which, to our knowledge, is the first attempt to describe this polysaccharide polymerization while preserving the mass balance relationships. Our model and method demonstrate the utility of a quasi-steady-state approach for inferring dynamic metabolic information in O. tauri directly from time-series gene expression data.
Published: 2011

29. Phylogenetic and biochemical evidence supports the recruitment of an ADP-glucose translocator for the export of photosynthate during plastid endosymbiosis

Author: Michael Handford, Andreas P.M. Weber, Marc Linka, Paul Dupree, Steven G. Ball, Philippe Deschamps, Christophe Colleoni, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Institute for Plant Biochemistry, Heinrich-Heine-Universität Düsseldorf [Düsseldorf], Ecologie Systématique et Evolution (ESE), Université Paris-Sud - Paris 11 (UP11)-AgroParisTech-Centre National de la Recherche Scientifique (CNRS), Departamento de Biologia, Universidad de Santiago de Chile [Santiago] (USACH), Department of Biochemistry, University of Cambridge [UK] (CAM), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf], and Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, Arabidopsis, Saccharomyces cerevisiae, Biology, Cyanobacteria, Nucleotide sugar, 01 natural sciences, Genome, Adenosine Diphosphate Glucose, 03 medical and health sciences, chemistry.chemical_compound, Genetics, Endomembrane system, Plastids, Photosynthesis, Plastid, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Symbiosis, Plastid envelope, Molecular Biology, Phylogeny, Ecology, Evolution, Behavior and Systematics, 030304 developmental biology, 0303 health sciences, Phylogenetic tree, Endosymbiosis, Starch, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Protein Transport, Biochemistry, chemistry, Nucleotide Transport Proteins, Cyanobiont, 010606 plant biology & botany
Abstract: International audience; The acquisition of photosynthesis by eukaryotic cells through enslavement of a cyanobacterium represents one of the most remarkable turning points in the history of life on Earth. In addition to endosymbiotic gene transfer, the acquisition of a protein import apparatus and the coordination of gene expression between host and endosymbiont genomes, the establishment of a metabolic connection was crucial for a functional endosymbiosis. It was previously hypothesized that the first metabolic connection between both partners of endosymbiosis was achieved through insertion of a host-derived metabolite transporter into the cyanobacterial plasma membrane. Reconstruction of starch metabolism in the common ancestor of photosynthetic eukaryotes suggested that ADP-glucose, a bacterial specific metabolite, was likely to be the photosynthate which was exported from the early cyanobiont. However, extant plastid transporters that have evolved from host-derived endomembrane transporters do not transport ADP-glucose but simple phosphorylated sugars in exchange for orthophosphate. We now show that those eukaryotic nucleotide sugar transporters, which define the closest relatives to the common ancestor of extant plastid envelope carbon translocators, possess an innate ability for transporting ADP-glucose. Such an unexpected ability would have been required to establish plastid endosymbiosis.
Published: 2010

30. Functions of heteromeric and homomeric isoamylase-type starch debranching enzymes in developing maize endosperm

Author: Steven G. Ball, Alan M. Myers, Jason R. Dinges, Qiaohui Lin, Ryan R. Lappe, Christophe Colleoni, Akiko Kubo, Alexander J. Meyer, Martha G. James, Tracie A. Hennen-Bierwagen, Joshua G. Rivenbark, Department of Genetics, Development, and Cell Biology, Iowa State University (ISU), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), and Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)
Subjects: 2. Zero hunger, 0106 biological sciences, Gel electrophoresis, 0303 health sciences, biology, Molecular mass, Physiology, Starch, Plant Science, 01 natural sciences, Isozyme, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Endosperm, 03 medical and health sciences, chemistry.chemical_compound, chemistry, Biochemistry, Genetics, biology.protein, Homomeric, Isoamylase, Amylase, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], 030304 developmental biology, 010606 plant biology & botany
Abstract: Functions of isoamylase-type starch-debranching enzyme (ISA) proteins and complexes in maize (Zea mays) endosperm were characterized. Wild-type endosperm contained three high molecular mass ISA complexes resolved by gel permeation chromatography and native-polyacrylamide gel electrophoresis. Two complexes of approximately 400 kD contained both ISA1 and ISA2, and an approximately 300-kD complex contained ISA1 but not ISA2. Novel mutations of sugary1 (su1) and isa2, coding for ISA1 and ISA2, respectively, were used to develop one maize line with ISA1 homomer but lacking heteromeric ISA and a second line with one form of ISA1/ISA2 heteromer but no homomeric enzyme. The mutations were su1-P, which caused an amino acid substitution in ISA1, and isa2-339, which was caused by transposon insertion and conditioned loss of ISA2. In agreement with the protein compositions, all three ISA complexes were missing in an ISA1-null line, whereas only the two higher molecular mass forms were absent in the ISA2-null line. Both su1-P and isa2-339 conditioned near-normal starch characteristics, in contrast to ISA-null lines, indicating that either homomeric or heteromeric ISA is competent for starch biosynthesis. The homomer-only line had smaller, more numerous granules. Thus, a function of heteromeric ISA not compensated for by homomeric enzyme affects granule initiation or growth, which may explain evolutionary selection for ISA2. ISA1 was required for the accumulation of ISA2, which is regulated posttranscriptionally. Quantitative polymerase chain reaction showed that the ISA1 transcript level was elevated in tissues where starch is synthesized and low during starch degradation, whereas ISA2 transcript was relatively abundant during periods of either starch biosynthesis or catabolism.
Published: 2010

31. Chlamydomonas starchless mutant defective in ADP-glucose pyrophosphorylase hyper-accumulates triacylglycerol

Author: David Dauvillée, Steven G. Ball, Danxiang Han, Yantao Li, Guongrong Hu, Qiang Hu, Milton Sommerfeld, Laboratory for Algae Research and Biotechnology (LARB), Arizona State University [Tempe] (ASU), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), and Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, Starch, Mutant, Bioengineering, Glucose-1-Phosphate Adenylyltransferase, Photosynthesis, 01 natural sciences, 7. Clean energy, Applied Microbiology and Biotechnology, Metabolic engineering, 03 medical and health sciences, chemistry.chemical_compound, 010608 biotechnology, Lipid Synthesis Pathway, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Triglycerides, 030304 developmental biology, 2. Zero hunger, 0303 health sciences, biology, Chlamydomonas, fungi, food and beverages, Lipid metabolism, biology.organism_classification, Lipid Metabolism, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], chemistry, Biochemistry, Biofuel, Biofuels, Mutation, Biotechnology
Abstract: International audience; Many microalgae and plants have the ability to synthesize large amounts of triacylglycerol (TAG) that can be used to produce biofuels. Presently, TAG-based biofuel production is limited by the feedstock supply. Metabolic engineering of lipid synthesis pathways to overproduce TAGs in oleaginous microalgae and oil crop plants has achieved only modest success. We demonstrate that inactivation of ADP-glucose pyrophosphorylase in a Chlamydomonas starchless mutant led to a 10-fold increase in TAG, suggesting that shunting of photosynthetic carbon partitioning from starch to TAG synthesis may represent a more effective strategy than direct manipulation of the lipid synthesis pathway to overproduce TAG.
Published: 2010

32. Engineering the chloroplast targeted malarial vaccine antigens in chlamydomonas starch granules

Author: David Dauvillée, Steven G. Ball, Sebastien Gruyer, Stanislas Tomavo, Christophe D'Hulst, Stéphane Delhaye, Christian Slomianny, Carole A. Long, Samuel E. Moretz, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 (CIIL), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS), Rôle des canaux ioniques membranaires et du calcium intracellulaire dans la physiopathologie de la prostate, Université de Lille, Sciences et Technologies-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Disease, National Institutes of Health, Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Centre d’Infection et d’Immunité de Lille (CIIL) - U1019 - UMR 8204 (CIIL), and Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, Plasmodium, Anatomy and Physiology, Chloroplasts, Starch, Chlamydomonas reinhardtii, 01 natural sciences, Mice, chemistry.chemical_compound, Immune Physiology, Molecular Cell Biology, Transgenes, chemistry.chemical_classification, Chlamydomonas Reinhardtii, 0303 health sciences, Multidisciplinary, biology, Vaccination, food and beverages, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], 3. Good health, Chloroplast, Infectious Diseases, Medicine, Genetic Engineering, Research Article, Biotechnology, Plasmids, Plant Cell Biology, Science, Bioengineering, Antigens, Protozoan, Polysaccharide, Microbiology, 03 medical and health sciences, Model Organisms, Starch Synthase, Antigen, Plant and Algal Models, Polysaccharides, 010608 biotechnology, Vaccine Development, Malaria Vaccines, parasitic diseases, Parasitic Diseases, Animals, Humans, Plasmodium Malariae, Plasmodium berghei, natural sciences, Antigens, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Biology, 030304 developmental biology, Chlamydomonas, fungi, Immunity, biology.organism_classification, Fusion protein, Malaria, chemistry, Immunoglobulin G, Clinical Immunology
Abstract: BackgroundMalaria, an Anopheles-borne parasitic disease, remains a major global health problem causing illness and death that disproportionately affects developing countries. Despite the incidence of malaria, which remains one of the most severe infections of human populations, there is no licensed vaccine against this life-threatening disease. In this context, we decided to explore the expression of Plasmodium vaccine antigens fused to the granule bound starch synthase (GBSS), the major protein associated to the starch matrix in all starch-accumulating plants and algae such as Chlamydomonas reinhardtii.Methods and findingsWe describe the development of genetically engineered starch granules containing plasmodial vaccine candidate antigens produced in the unicellular green algae Chlamydomonas reinhardtii. We show that the C-terminal domains of proteins from the rodent Plasmodium species, Plasmodium berghei Apical Major Antigen AMA1, or Major Surface Protein MSP1 fused to the algal granule bound starch synthase (GBSS) are efficiently expressed and bound to the polysaccharide matrix. Mice were either immunized intraperitoneally with the engineered starch particles and Freund adjuvant, or fed with the engineered particles co-delivered with the mucosal adjuvant, and challenged intraperitoneally with a lethal inoculum of P. Berghei. Both experimental strategies led to a significantly reduced parasitemia with an extension of life span including complete cure for intraperitoneal delivery as assessed by negative blood thin smears. In the case of the starch bound P. falciparum GBSS-MSP1 fusion protein, the immune sera or purified immunoglobulin G of mice immunized with the corresponding starch strongly inhibited in vitro the intra-erythrocytic asexual development of the most human deadly plasmodial species.ConclusionThis novel system paves the way for the production of clinically relevant plasmodial antigens as algal starch-based particles designated herein as amylosomes, demonstrating that efficient production of edible vaccines can be genetically produced in Chlamydomonas.
Published: 2010

33. Genetic dissection of floridean starch synthesis in the cytosol of the model dinoflagellate Crypthecodinium cohnii

Author: David Dauvillée, Jimi Devassine, Philippe Deschamps, Amandine Durand-Terrasson, Aline Devin, Steven G. Ball, Jean-Philippe Ral, Jean-Luc Putaux, Charlotte Plancke, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), CSIRO Plant Industry, Commonwealth Scientific and Industrial Research Organisation [Canberra] (CSIRO), Centre de Recherches sur les Macromolécules Végétales (CERMAV), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), inconnu, Inconnu, Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Université de Lille-Centre National de la Recherche Scientifique (CNRS), and Université Joseph Fourier - Grenoble 1 (UJF)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, Uridine Diphosphate Glucose, Starch, Red algae, Biology, 01 natural sciences, 03 medical and health sciences, chemistry.chemical_compound, Cytosol, Starch Synthase, Botany, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Plastid, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, Multidisciplinary, Archaeplastida, Starch synthase activity, food and beverages, Crypthecodinium cohnii, Biological Sciences, biology.organism_classification, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], chemistry, Biochemistry, Mutation, biology.protein, Dinoflagellida, Green algae, Starch synthase, 010606 plant biology & botany
Abstract: Starch defines an insoluble semicrystalline form of storage polysaccharides restricted to Archaeplastida (red and green algae, land plants, and glaucophytes) and some secondary endosymbiosis derivatives of the latter. While green algae and land-plants store starch in plastids by using an ADP-glucose-based pathway related to that of cyanobacteria, red algae, glaucophytes, cryptophytes, dinoflagellates, and apicomplexa parasites store a similar type of polysaccharide named floridean starch in their cytosol or periplast. These organisms are suspected to store their floridean starch from UDP-glucose in a fashion similar to heterotrophic eukaryotes. However, experimental proof of this suspicion has never been produced. Dinoflagellates define an important group of both photoautotrophic and heterotrophic protists. We now report the selection and characterization of a low starch mutant of the heterotrophic dinoflagellate Crypthecodinium cohnii . We show that the sta1-1 mutation of C. cohnii leads to a modification of the UDP-glucose-specific soluble starch synthase activity that correlates with a decrease in starch content and an alteration of amylopectin structure. These experimental results validate the UDP-glucose-based pathway proposed for floridean starch synthesis.
Published: 2009

34. Further Evidence for the Mandatory Nature of Polysaccharide Debranching for the Aggregation of Semi-Crystalline Starch and for Overlapping Functions of Debranching Enzymes in Arabidopsis Leaves

Author: Fabrice Wattebled, Nicolas Szydlowski, Christophe D'Hulst, Aline Devin, Steven G. Ball, Véronique Planchot, Bruno Pontoire, Ying Dong, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Biopolymeres, Interactions, Assemblages, Institut National de la Recherche Agronomique (INRA), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Université de Lille-Centre National de la Recherche Scientifique (CNRS), and Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA)
Subjects: 0106 biological sciences, Physiology, Starch, ISOAMYLASE, Arabidopsis, ENZYME DEBRANCHANTE, ISOFORMS, Plant Science, Polysaccharide, 01 natural sciences, 03 medical and health sciences, chemistry.chemical_compound, Polysaccharides, PULLULANASE, ENZYMATIC ACTIVITY, Genetics, Arabidopsis thaliana, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], 030304 developmental biology, DNA Primers, chemistry.chemical_classification, 0303 health sciences, biology, Pullulanase, Base Sequence, Reverse Transcriptase Polymerase Chain Reaction, ENZYMATIC SPECIFICITY, Wild type, DEBRANCHING ENZYME, biology.organism_classification, Enzymes, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Plant Leaves, Enzyme, chemistry, Biochemistry, Crystallization, STARCH METABOLISM, Function (biology), 010606 plant biology & botany, Research Article
Abstract: Four isoforms of debranching enzymes are found in the genome of Arabidopsis (Arabidopsis thaliana): three isoamylases (ISA1, ISA2, and ISA3) and a pullulanase (PU1). Each isoform has a specific function in the starch pathway: synthesis and/or degradation. In this work we have determined the levels of functional redundancy existing between these isoforms by producing and analyzing different combinations of mutations: isa3-1 pu1-1, isa1-1 isa3-1, and isa1-1 isa3-1 pu1-1. While the starch content strongly increased in the isa3-1 pu1-1 double mutant, the latter decreased by over 98% in the isa1-1 isa3-1 genotype and almost vanished in triple mutant combination. In addition, whereas the isa3-1 pu1-1 double mutant synthesizes starch very similar to that of the wild type, the structure of the residual starch present either in isa1-1 isa3-1 or in isa1-1 isa3-1 pu1-1 combination is deeply affected. In the same way, water-soluble polysaccharides that accumulate in the isa1-1 isa3-1 and isa1-1 isa3-1 pu1-1 genotypes display strongly modified structure compared to those found in isa1-1. Taken together, these results show that in addition to its established function in polysaccharide degradation, the activity of ISA3 is partially redundant to that of ISA1 for starch synthesis. Our results also reveal the dual function of pullulanase since it is partially redundant to ISA3 for degradation and to ISA1 for synthesis. Finally, x-ray diffraction analyses suggest that the crystallinity and the presence of the 9- to 10-nm repetition pattern in starch precisely depend on the level of debranching enzyme activity.
Published: 2008

35. The heterotrophic dinoflagellate Crypthecodinium cohnii defines a model genetic system to investigate cytoplasmic starch synthesis

Author: Sophie Haebel, Jean-Luc Putaux, Evelyne Derelle, Aline Devin, Steven G. Ball, Jimi Devassine, David Dauvillée, Charlotte Plancke, Stanislas Tomavo, Marie-Christine Slomianny, Christophe Colleoni, Philippe Deschamps, Delphine Guillebeault, Alain Buléon, Hervé Moreau, Martin Steup, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Laboratoire d'océanographie biologique de Banyuls (LOBB), Observatoire océanologique de Banyuls (OOB), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS), Center of Mass Spectrometry of Biopolymers and Plant Physiology, University of Potsdam = Universität Potsdam, Plant Physiology, Institute of Biochemistry and Biology, Institut National de la Recherche Agronomique, Centre de Recherches Agroalimentaires, Institut National de la Recherche Agronomique (INRA), Centre de Recherches sur les Macromolécules Végétales (CERMAV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), University of Potsdam, Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences de l'Univers (INSU - CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Observatoire océanologique de Banyuls (OOB), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), and Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)
Subjects: 0106 biological sciences, Cytoplasm, DINOFLAGELLATE, STRUCTURE, Starch, CRYPTHECODINIUM COHNII, Protozoan Proteins, 01 natural sciences, DINOFLAGELLATA, chemistry.chemical_compound, Amylose, Recombination, Genetic, chemistry.chemical_classification, 0303 health sciences, Starch phosphorylase, biology, food and beverages, Starch Phosphorylase, Articles, General Medicine, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Biochemistry, Amylopectin, Dinoflagellida, STARCH, Starch synthase, Uridine Diphosphate Glucose, METABOLISM, Polysaccharide, Microbiology, 03 medical and health sciences, Starch Synthase, GENETIC MARKER, Animals, BIOSYNTHESIS, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Molecular Biology, Crosses, Genetic, 030304 developmental biology, Models, Genetic, Algal Proteins, Dinoflagellate, Heterotrophic Processes, Crypthecodinium cohnii, biology.organism_classification, MODEL, chemistry, Mutagenesis, biology.protein, 010606 plant biology & botany
Abstract: The nature of the cytoplasmic pathway of starch biosynthesis was investigated in the model heterotrophic dinoflagellate Crypthecodinium cohnii . The storage polysaccharide granules were shown to be composed of both amylose and amylopectin fractions with a chain length distribution and crystalline organization very similar to those of green algae and land plant starch. Preliminary characterization of the starch pathway demonstrated that C. cohnii contains multiple forms of soluble starch synthases and one major 110-kDa granule-bound starch synthase. All purified enzymes displayed a marked substrate preference for UDP-glucose. At variance with most other microorganisms, the accumulation of starch in the dinoflagellate occurs during early and mid-log phase, with little or no synthesis witnessed when approaching stationary phase. In order to establish a genetic system allowing the study of cytoplasmic starch metabolism in eukaryotes, we describe the isolation of marker mutations and the successful selection of random recombinant populations after homothallic crosses.
Published: 2008

36. Early Gene Duplication within Chloroplastida and its correspondence with Relocation of Starch Metabolism to Chloroplasts

Author: Steven G. Ball, David Dauvillée, Hervé Moreau, Alexandra Z. Worden, Philippe Deschamps, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Laboratoire d'océanographie biologique de Banyuls (LOBB), Observatoire océanologique de Banyuls (OOB), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS), Monterey Bay Aquarium Research Institute (MBARI), Monterey Bay Aquarium Research Institute, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences de l'Univers (INSU - CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Observatoire océanologique de Banyuls (OOB), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), and Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, Chloroplasts, Chlamydomonas reinhardtii, Oligosaccharides, Investigations, 01 natural sciences, Ostreococcus, 03 medical and health sciences, Volvox, Gene Duplication, Genetics, Glaucophyta, Plastid, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Phylogeny, 030304 developmental biology, 2. Zero hunger, 0303 health sciences, biology, Endosymbiosis, Archaeplastida, Eukaryota, Membrane Transport Proteins, food and beverages, Starch, biology.organism_classification, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Chloroplast, Adenosine Diphosphate, Isoenzymes, Glucose, Biochemistry, 010606 plant biology & botany
Abstract: The endosymbiosis event resulting in the plastid of photosynthetic eukaryotes was accompanied by the appearance of a novel form of storage polysaccharide in Rhodophyceae, Glaucophyta, and Chloroplastida. Previous analyses indicated that starch synthesis resulted from the merging of the cyanobacterial and the eukaryotic storage polysaccharide metabolism pathways. We performed a comparative bioinformatic analysis of six algal genome sequences to investigate this merger. Specifically, we analyzed two Chlorophyceae, Chlamydomonas reinhardtii and Volvox carterii, and four Prasinophytae, two Ostreococcus strains and two Micromonas pusilla strains. Our analyses revealed a complex metabolic pathway whose intricacies and function seem conserved throughout the green lineage. Comparison of this pathway to that recently proposed for the Rhodophyceae suggests that the complexity that we observed is unique to the green lineage and was generated when the latter diverged from the red algae. This finding corresponds well with the plastidial location of starch metabolism in Chloroplastidae. In contrast, Rhodophyceae and Glaucophyta produce and store starch in the cytoplasm and have a lower complexity pathway. Cytoplasmic starch synthesis is currently hypothesized to represent the ancestral state of storage polysaccharide metabolism in Archaeplastida. The retargeting of components of the cytoplasmic pathway to plastids likely required a complex stepwise process involving several rounds of gene duplications. We propose that this relocation of glucan synthesis to the plastid facilitated evolution of chlorophyll-containing light-harvesting complex antennae by playing a protective role within the chloroplast.
Published: 2008

37. Variation in Storage {alpha}-Glucans of the Porphyridiales (Rhodophyta)

Author: Akiko Yokoyama, Alain Buléon, Christophe Colleoni, Naoko Fujita, Yoshiaki Hara, Yasunori Oyama, Jean-Luc Putaux, Yasunori Nakamura, Steven G. Ball, Mikio Tsuzuki, Aya Satoh, Shoko Fujiwara, Mai Konishi, Takahiro Shimonaga, Graduate School of Agricultural and Life Sciences [UTokyo] (GSALS), The University of Tokyo (UTokyo), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique, Centre de Recherches Agroalimentaires, Institut National de la Recherche Agronomique (INRA), Centre de Recherches sur les Macromolécules Végétales (CERMAV), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), Department of Global Agricultural Sciences Graduate School of Agricultural and Life Sciences, The University of Tokyo, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Université de Lille-Centre National de la Recherche Scientifique (CNRS), and Université Joseph Fourier - Grenoble 1 (UJF)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, Physiology, Starch, Plant Science, Biology, GLYCOGEN, 01 natural sciences, RHODOPHYTA, Gel permeation chromatography, 03 medical and health sciences, chemistry.chemical_compound, Algae, Amylose, Botany, Carbohydrate Conformation, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Glycogen synthase, Glucans, 030304 developmental biology, Glucan, chemistry.chemical_classification, 0303 health sciences, Glycogen, Galdieria sulphuraria, PORPHYRIDIUM, Cell Biology, General Medicine, biology.organism_classification, FLORIDEAN STARCH, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], AMYLOSE, carbohydrates (lipids), chemistry, Biochemistry, biology.protein, PORPHYRIDIALES, ALGUE ROUGE, SEMI-AMYLOPECTIN, 010606 plant biology & botany
Abstract: Storage glucans were analyzed in the Porphyridiales which include the most primitive and phylogenetically diverged species in the Rhodophyta, to understand early evolution of the glucan structure in the Rhodophyta. The storage glucans of both Galdieria sulphuraria and Cyanidium caldarium consisted of glycogen, while those of Rhodosorus marinus, Porphyridium purpureum, P. sordidum and Rhodella violacea could be defined as semi-amylopectin. X-ray diffraction analysis of the glucans demonstrated variation in the crystalline structure: the patterns in P. purpureum and R. violacea were of A- and B-types, respectively, while alpha-glucans of R. marinus and P. sordidum displayed structures with lower crystallinity. Electron microscopic observations indicated that the alpha-glucans of P. sordidum consisted of two kinds of granules; a minor component of more dense granules with crystalline leaflets and a major component of softer ones without crystalline structure. Gel permeation chromatography showed that all the species containing the semi-amylopectin-type glucans also contained amylose, although the relative amounts of this fraction were different depending on the species. Our results are consistent with two distinct evolution scenarios defined either by the independent acquisition of semi-crystalline starch-like structures in the different plant lineages or more probably by the loss of starch and reversion to glycogen synthesis in cyanidian algae growing in hot and acid environments.
Published: 2008

38. THE PATHWAY OF CYTOSOLIC STARCH SYNTHESIS IN THE MODEL GLAUCOPHYTE CYANOPHORA PARADOXA

Author: Steven G. Ball, Charlotte Plancke, Wolfgang Löffelhardt, Jean-Philippe Ral, Danielle Dupeyre, Jean-Luc Putaux, David Dauvillée, Sophie Haebel, Christophe Colleoni, Alain Buléon, Yasunori Nakamura, Philippe Deschamps, Christophe D'Hulst, Gehrardt Ritte, Martin Steup, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Graduate School of Agricultural and Life Sciences [UTokyo] (GSALS), The University of Tokyo (UTokyo), Center of Mass Spectrometry of Biopolymers and Plant Physiology, University of Potsdam, Plant Physiology, Institute of Biochemistry and Biology, Institut National de la Recherche Agronomique, Centre de Recherches Agroalimentaires, Institut National de la Recherche Agronomique (INRA), Centre de Recherches sur les Macromolécules Végétales (CERMAV), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Department of Global Agricultural Sciences Graduate School of Agricultural and Life Sciences, The University of Tokyo, Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Université de Lille-Centre National de la Recherche Scientifique (CNRS), University of Potsdam = Universität Potsdam, and Université Joseph Fourier - Grenoble 1 (UJF)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)
Subjects: Uridine Diphosphate Glucose, 0106 biological sciences, DNA, Complementary, ENZYME, STRUCTURE, Starch, Cyanophora, Biology, Models, Biological, 01 natural sciences, Microbiology, CYANOPHORA PARADOXA, UDP-GLUCOSE, 03 medical and health sciences, chemistry.chemical_compound, METABOLIC PATHWAY, Cytosol, Amylose, Isoamylase, BIOSYNTHESIS, Cloning, Molecular, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Molecular Biology, Phylogeny, 030304 developmental biology, 0303 health sciences, Starch phosphorylase, food and beverages, Starch Phosphorylase, Articles, General Medicine, STARCH SYNTHASE, biology.organism_classification, AMYLOPECTIN, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], GLAUCOPHYTA, chemistry, Biochemistry, Amylopectin, biology.protein, STARCH, Cyanophora paradoxa, Starch synthase, 010606 plant biology & botany
Abstract: The nature of the cytoplasmic pathway of starch biosynthesis was investigated in the model glaucophyte Cyanophora paradoxa . The storage polysaccharide granules are shown to be composed of both amylose and amylopectin fractions, with a chain length distribution and crystalline organization similar to those of green algae and land plant starch. A preliminary characterization of the starch pathway demonstrates that Cyanophora paradoxa contains several UDP-glucose-utilizing soluble starch synthase activities related to those of the Rhodophyceae. In addition, Cyanophora paradoxa synthesizes amylose with a granule-bound starch synthase displaying a preference for UDP-glucose. A debranching enzyme of isoamylase specificity and multiple starch phosphorylases also are evidenced in the model glaucophyte. The picture emerging from our biochemical and molecular characterizations consists of the presence of a UDP-glucose-based pathway similar to that recently proposed for the red algae, the cryptophytes, and the alveolates. The correlative presence of isoamylase and starch among photosynthetic eukaryotes is discussed.
Published: 2007

39. Genome analysis of the smallest free-living eukaryote Ostreococcus tauri unveils many unique features

Author: Bernard De Baets, Yves Van de Peer, Benoît Piégu, Chris Bowler, Kamel Jabbari, Frédéric Partensky, Evelyne Derelle, Richard G. Cooke, Pierre Rouzé, Sophie Echeynié, André Picard, François-Yves Bouget, Conchita Ferraz, Gwenael Piganeau, Stephane Rombauts, Sven Degroeve, Alexandra Z. Worden, Hervé Moreau, Jacques G. Demaille, Jean-Philippe Ral, Michel Delseny, Steven G. Ball, Yvan Saeys, Olivier Panaud, Jan Wuyts, Steven Robbens, Modèles en biologie cellulaire et évolutive (MBCE), Observatoire océanologique de Banyuls (OOB), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Institut de génétique humaine (IGH), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Center for Plant Systems Biology (PSB Center), Vlaams Instituut voor Biotechnologie [Ghent, Belgique] (VIB), Adaptation et diversité en milieu marin (AD2M), Station biologique de Roscoff [Roscoff] (SBR), Laboratoire Génome et développement des plantes (LGDP), and Université de Perpignan Via Domitia (UPVD)-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, Genome evolution, MESH: Sequence Analysis, DNA, Nuclear gene, Lineage (genetic), Gene prediction, 01 natural sciences, Genome, MESH: Eukaryotic Cells, Ostreococcus tauri, Ostreococcus, [SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics, 03 medical and health sciences, MESH: Algae, Green, Gene density, Animals, MESH: Animals, MESH: Genome, Photosynthesis, MESH: Evolution, Molecular, 030304 developmental biology, Genetics, 0303 health sciences, Multidisciplinary, MESH: Molecular Sequence Data, biology, Biological Sciences, biology.organism_classification, Phytoplankton, MESH: Chromosomes, 010606 plant biology & botany
Abstract: The green lineage is reportedly 1,500 million years old, evolving shortly after the endosymbiosis event that gave rise to early photosynthetic eukaryotes. In this study, we unveil the complete genome sequence of an ancient member of this lineage, the unicellular green alga Ostreococcus tauri (Prasinophyceae). This cosmopolitan marine primary producer is the world’s smallest free-living eukaryote known to date. Features likely reflecting optimization of environmentally relevant pathways, including resource acquisition, unusual photosynthesis apparatus, and genes potentially involved in C 4 photosynthesis, were observed, as was downsizing of many gene families. Overall, the 12.56-Mb nuclear genome has an extremely high gene density, in part because of extensive reduction of intergenic regions and other forms of compaction such as gene fusion. However, the genome is structurally complex. It exhibits previously unobserved levels of heterogeneity for a eukaryote. Two chromosomes differ structurally from the other eighteen. Both have a significantly biased G+C content, and, remarkably, they contain the majority of transposable elements. Many chromosome 2 genes also have unique codon usage and splicing, but phylogenetic analysis and composition do not support alien gene origin. In contrast, most chromosome 19 genes show no similarity to green lineage genes and a large number of them are specialized in cell surface processes. Taken together, the complete genome sequence, unusual features, and downsized gene families, make O. tauri an ideal model system for research on eukaryotic genome evolution, including chromosome specialization and green lineage ancestry.
Published: 2006

40. Nature of the periplastidial pathway of starch synthesis in the cryptophyte Guillardia theta

Author: Sophie Haebel, David Dauvillée, Ilka Haferkamp, Christophe Colleoni, H. Ekkehard Neuhaus, Uwe Maier, Christophe D'Hulst, Steven G. Ball, Jean-Luc Putaux, Martin Steup, Charlotte Plancke, Alain Buléon, Sven B. Gould, Philippe Deschamps, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Pflanzenphysiologie, Fachbereich Biologie, Technische Universitat Kaiserslautern, Technische Universität Kaiserslautern (TU Kaiserslautern), Center of Mass Spectrometry of Biopolymers and Plant Physiology, University of Potsdam, Plant Physiology, Institute of Biochemistry and Biology, Institut National de la Recherche Agronomique, Centre de Recherches Agroalimentaires, Institut National de la Recherche Agronomique (INRA), Centre de Recherches sur les Macromolécules Végétales (CERMAV), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Philipps Universität Marbug, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS), Philipps Universität Marburg, Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), University of Potsdam = Universität Potsdam, Université Joseph Fourier - Grenoble 1 (UJF)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), and Philipps Universität Marburg = Philipps University of Marburg
Subjects: 0106 biological sciences, MESH: Amylopectin, Starch, Amylopectin, MESH: Amino Acid Sequence, 01 natural sciences, Pyrenoid, chemistry.chemical_compound, MESH: Cryptophyta, Amylose, Plastids, MESH: Phylogeny, Phylogeny, chemistry.chemical_classification, 0303 health sciences, biology, food and beverages, MESH: Amylose, Articles, General Medicine, MESH: Plastids, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Biochemistry, Glucosyltransferases, Starch synthase, Cryptophyta, Signal peptide, MESH: Starch, Molecular Sequence Data, MESH: Cytoplasmic Granules, Polysaccharide, Cytoplasmic Granules, Microbiology, 03 medical and health sciences, Starch Synthase, Amino Acid Sequence, Plastid, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Molecular Biology, Institut für Biochemie und Biologie, 030304 developmental biology, MESH: Glucosyltransferases, MESH: Molecular Sequence Data, chemistry, biology.protein, MESH: Starch Synthase, 010606 plant biology & botany
Abstract: The nature of the periplastidial pathway of starch biosynthesis was investigated with the model cryptophyte Guillardia theta . The storage polysaccharide granules were shown to be composed of both amylose and amylopectin fractions with a chain length distribution and crystalline organization very similar to those of starch from green algae and land plants. Most starch granules displayed a shape consistent with biosynthesis occurring around the pyrenoid through the rhodoplast membranes. A protein with significant similarity to the amylose-synthesizing granule-bound starch synthase 1 from green plants was found as the major polypeptide bound to the polysaccharide matrix. N-terminal sequencing of the mature protein proved that the precursor protein carries a nonfunctional transit peptide in its bipartite topogenic signal sequence which is cleaved without yielding transport of the enzyme across the two inner plastid membranes. The enzyme was shown to display similar affinities for ADP and UDP-glucose, while the V max measured with UDP-glucose was twofold higher. The granule-bound starch synthase from Guillardia theta was demonstrated to be responsible for the synthesis of long glucan chains and therefore to be the functional equivalent of the amylose-synthesizing enzyme of green plants. Preliminary characterization of the starch pathway suggests that Guillardia theta utilizes a UDP-glucose-based pathway to synthesize starch.
Published: 2006

41. Mutants of Arabidopsis lacking starch branching enzyme II substitute plastidial starch synthesis by cytoplasmic maltose accumulation

Author: Véronique Planchot, Fabrice Wattebled, Sylvain Dumez, David Dauvillée, David Delvallé, Steven G. Ball, Christophe D'Hulst, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), IFR 118 (UPRES EA 1033), Université de Lille, Sciences et Technologies, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Unité de recherche sur les polysaccharides, leurs organisations et interactions (URPOI), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Unite de Recherche sur les Polysaccharides leurs Interactions et leurs Organisations, and Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, Starch, Mutant, Arabidopsis, Plant Science, 01 natural sciences, [SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics, 03 medical and health sciences, chemistry.chemical_compound, 1,4-alpha-Glucan Branching Enzyme, Glycogen branching enzyme, BIOSYNTHESIS, Plastids, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Maltose, Research Articles, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, biology, food and beverages, Cell Biology, biology.organism_classification, STARCH BRANCHING ENZYME, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], CYTOPLASM, Mutagenesis, Insertional, Enzyme, chemistry, Biochemistry, Cytoplasm, Amylopectin, Mutation, Chromatography, Gel, biology.protein, STARCH, 010606 plant biology & botany
Abstract: Three genes, BE1, BE2, and BE3, which potentially encode isoforms of starch branching enzymes, have been found in the genome of Arabidopsis thaliana. Although no impact on starch structure was observed in null be1 mutants, modifications in amylopectin structure analogous to those of other branching enzyme II mutants were detected in be2 and be3. No impact on starch content was found in any of the single mutant lines. Moreover, three double mutant combinations were produced (be1 be2, be1 be3, and be2 be3), and the impact of the mutations on starch content and structure was analyzed. Our results suggest that BE1 has no apparent function for the synthesis of starch in the leaves, as both be1 be2 and be1 be3 double mutants display the same phenotype as be2 and be3 separately. However, starch synthesis was abolished in be2 be3, while high levels of α-maltose were assayed in the cytosol. This result indicates that the functions of both BE2 and BE3, which belong to class II starch branching enzymes, are largely redundant in Arabidopsis. Moreover, we demonstrate that maltose accumulation depends on the presence of an active ADP-glucose pyrophosphorylase and that the cytosolic transglucosidase DISPROPORTIONATING ENZYME2, required for maltose metabolization, is specific for β-maltose.
Published: 2006

42. Circadian clock regulation of starch metabolism establishes GBSSI as a major contributor to amylopectin synthesis in Chlamydomonas reinhardtii

Author: Ravindra N. Chibbar, Philippe Deschamps, Fabrice Wattebled, Christophe D'Hulst, Saul Purton, Jean-Philippe Ral, David Dauvillée, Matthew K. Morell, Christophe Colleoni, Steven G. Ball, Clément Nempont, Zhongyi Li, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), CSIRO Plant Industry, Commonwealth Scientific and Industrial Research Organisation [Canberra] (CSIRO), Plant Biotechnology Institute, National Research Council of Canada (NRC), Department of Biology, University College of London [London] (UCL), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), and Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, Physiology, Starch, Amylopectin, Genes, Protozoan, Molecular Sequence Data, Circadian clock, Chlamydomonas reinhardtii, Glucose-1-Phosphate Adenylyltransferase, Plant Science, Polysaccharide, 01 natural sciences, 03 medical and health sciences, chemistry.chemical_compound, Starch Synthase, Biological Clocks, Amylose, Genetics, Animals, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], 030304 developmental biology, Glucan, chemistry.chemical_classification, 0303 health sciences, biology, food and beverages, biology.organism_classification, Circadian Rhythm, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], chemistry, Biochemistry, Glucosyltransferases, biology.protein, Starch synthase, Research Article, 010606 plant biology & botany
Abstract: Chlamydomonas reinhardtii displays a diurnal rhythm of starch content that peaks in the middle of the night phase if the algae are provided with acetate and CO2 as a carbon source. We show that this rhythm is controlled by the circadian clock and is tightly correlated to ADP-glucose pyrophosphorylase activity. Persistence of this rhythm depends on the presence of either soluble starch synthase III or granule-bound starch synthase I (GBSSI). We show that both enzymes play a similar function in synthesizing the long glucan fraction that interconnects the amylopectin clusters. We demonstrate that in log phase-oscillating cultures, GBSSI is required to obtain maximal polysaccharide content and fully compensates for the loss of soluble starch synthase III. A point mutation in the GBSSI gene that prevents extension of amylopectin chains, but retains the enzyme's normal ability to extend maltooligosaccharides, abolishes the function of GBSSI both in amylopectin and amylose synthesis and leads to a decrease in starch content in oscillating cultures. We propose that GBSSI has evolved as a major enzyme of amylopectin synthesis and that amylose synthesis comes as a secondary consequence of prolonged synthesis by GBSSI in arrhythmic systems. Maintenance in higher plant leaves of circadian clock control of GBSSI transcription is discussed.
Published: 2006

43. Glycogen Phosphorylase, the Product of the glgP Gene, Catalyzes Glycogen Breakdown by Removing Glucose Units from the Nonreducing Ends in Escherichia coli

Author: David Dauvillée, Nora Alonso-Casajús, Steven G. Ball, Francisco Muñoz, Gustavo Eydallin, Javier Pozueta-Romero, María Teresa Morán-Zorzano, Alejandro M. Viale, Edurne Baroja-Fernández, Agrobioteknologiako Instituta, Nafarroako Unibertsitate Publikoa and Consejo Superior de Investigaciones Cientificas, Universidad Pública de Navarra [Espagne] = Public University of Navarra (UPNA), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Instituto de Biología Molecular y Celular de Rosario [Rosario] (IBR), Consejo Nacional de Investigaciones Científicas y Técnicas [Buenos Aires] (CONICET)-Universidad Nacional de Rosario [Santa Fe], IdAB – Instituto de Agrobiotecnología / Agrobioteknologiako Institutua, Universidad Pública de Navarra / Nafarroako Unibertsitate Publikoa, Universidad Pública de Navarra [Espagne] (UPNA), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), and Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: Genotype, Physiology and Metabolism, Molecular Sequence Data, Biology, medicine.disease_cause, Polysaccharide, Microbiology, Glycogen debranching enzyme, 03 medical and health sciences, chemistry.chemical_compound, Glycogen phosphorylase, medicine, Glycogen branching enzyme, Escherichia coli, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Phosphorylase kinase, Glycogen synthase, Molecular Biology, DNA Primers, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Base Sequence, Glycogen, 030306 microbiology, Escherichia coli Proteins, Glycogen Phosphorylase, Polysaccharides, Bacterial, Molecular biology, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Kinetics, Bacterial glycogen phosphorylase (GlgP), Glucose, chemistry, Biochemistry, biology.protein
Abstract: To understand the biological function of bacterial glycogen phosphorylase (GlgP), we have produced and characterized Escherichia coli cells with null or altered glgP expression. glgP deletion mutants (Δ glgP ) totally lacked glycogen phosphorylase activity, indicating that all the enzymatic activity is dependent upon the glgP product. Moderate increases of glycogen phosphorylase activity were accompanied by marked reductions of the intracellular glycogen levels in cells cultured in the presence of glucose. In turn, both glycogen content and rates of glycogen accumulation in ΔglgP cells were severalfold higher than those of wild-type cells. These defects correlated with the presence of longer external chains in the polysaccharide accumulated by ΔglgP cells. The overall results thus show that GlgP catalyzes glycogen breakdown and affects glycogen structure by removing glucose units from the polysaccharide outer chains in E. coli .
Published: 2006

44. Control of starch biosynthesis in vascular plants and algae

Author: Zhongyi Li, S. Rahman, Christophe D'Hulst, Ahmed Regina, Steven G. Ball, Matthew K. Morell, CSIRO Plant Industry, Commonwealth Scientific and Industrial Research Organisation [Canberra] (CSIRO), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), and Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)
Subjects: chemistry.chemical_compound, Algae, biology, Biosynthesis, Germination, Chemistry, Botany, Carbohydrate, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], biology.organism_classification, Starch biosynthesis, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]
Published: 2006

45. Mutants of Arabidopsis Lacking a Chloroplastic Isoamylase Accumulate Phytoglycogen and an Abnormal Form of Amylopectin

Author: Pierre Berbezy, Steven G. Ball, Fabrice Wattebled, Paul Colonna, Ying Dong, Christophe D'Hulst, Véronique Planchot, Manash Chatterjee, Sylvain Dumez, Darshna Vyas, David Delvallé, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Unité de recherche sur les polysaccharides, leurs organisations et interactions (URPOI), Institut National de la Recherche Agronomique (INRA), Biogemma UK Ltd, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Biogemma UK Limited, Partenaires INRAE, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Unite de Recherche sur les Polysaccharides leurs Interactions et leurs Organisations, and Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, Physiology, Mutant, STARCH DEBRANCHING ENZYME, Plant Science, Biology, Polysaccharide, 01 natural sciences, Isoamylase activity, Glycogen debranching enzyme, [SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics, 03 medical and health sciences, chemistry.chemical_compound, Genetics, Isoamylase, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Phytoglycogen, Wild type, food and beverages, AMYLOPECTIN, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], chemistry, Biochemistry, Amylopectin, STARCH, 010606 plant biology & botany
Abstract: Mutant lines defective for each of the four starch debranching enzyme (DBE) genes (AtISA1, AtISA2, AtISA3, and AtPU1) detected in the nuclear genome of Arabidopsis (Arabidopsis thaliana) were produced and analyzed. Our results indicate that both AtISA1 and AtISA2 are required for the production of a functional isoamylase-type of DBE named Iso1, the major isoamylase activity found in leaves. The absence of Iso1 leads to an 80% decrease in the starch content in both lines and to the accumulation of water-soluble polysaccharides whose structure is similar to glycogen. In addition, the residual amylopectin structure in the corresponding mutant lines displays a strong modification when compared to the wild type, suggesting a direct, rather than an indirect, function of Iso1 during the synthesis of amylopectin. Mutant lines carrying a defect in AtISA3 display a strong starch-excess phenotype at the end of both the light and the dark phases accompanied by a small modification of the amylopectin structure. This result suggests that this isoamylase-type of DBE plays a major role during starch mobilization. The analysis of the Atpu1 single-mutant lines did not lead to a distinctive phenotype. However, Atisa2/Atpu1 double-mutant lines display a 92% decrease in starch content. This suggests that the function of pullulanase partly overlaps that of Iso1, although its implication remains negligible when Iso1 is present within the cell.
Published: 2005

46. Amylopectin biogenesis and characterization in the protozoan parasite Toxoplasma gondii, the intracellular development of which is restricted in the HepG2 cell line

Author: Denis Leleu, Alexandra Coppin, Yann Guérardel, Luc Liénard, Stanislas Tomavo, Christian Slomianny, Gérard Strecker, Steven G. Ball, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Rôle des canaux ioniques membranaires et du calcium intracellulaire dans la psysiopathologie de la prostate, Institut National de la Santé et de la Recherche Médicale (INSERM), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), and Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)
Subjects: Amylopectin, Immunology, Biology, Polysaccharide, Microbiology, Mass Spectrometry, Cell Line, Apicomplexa, chemistry.chemical_compound, Cell Line, Tumor, parasitic diseases, Animals, Humans, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], chemistry.chemical_classification, Life Cycle Stages, Glycogen, Toxoplasma gondii, food and beverages, biology.organism_classification, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], carbohydrates (lipids), Microscopy, Electron, Infectious Diseases, chemistry, Biochemistry, Cytoplasm, Protozoa, Toxoplasma, Biogenesis
Abstract: The obligate intracellular protozoan Toxoplasma gondii belongs to the phylum Apicomplexa, which is composed of numerous parasites causing major diseases such as malaria, toxoplasmosis and coccidiosis. The life cycle of T. gondii involves developmental processes from one stage to another with both asexual and sexual parasitic forms. Throughout their life cycle, some apicomplexan parasites accumulate a crystalline storage polysaccharide analogous to amylopectin within the cytoplasm. In T. gondii, both the slowly dividing encysted bradyzoites and the sporozoites of the sexual stage contain a high number of amylopectin granules (AG), while the rapidly replicating tachyzoites are devoid of amylopectin. It is thought that this storage polysaccharide may represent an energy reserve that could fuel the transition from one developmental stage to another one. At present, by comparison to glycogen and plant starch, little is known about the biosynthesis, structure and biological functions of amylopectin in T. gondii. Here, we describe an in vitro system allowing the production and purification of a large amount of amylopectin, which has been subjected to detailed biochemical and structural analyses. Our data indicate that T. gondii synthesizes a genuine amylopectin following changes in the environmental conditions and that this storage polysaccharide differs from glycogen and starch in terms of glucan chain length.
Published: 2005

47. Evolution of plant-like crystalline storage polysaccharide in the protozoan parasite Toxoplasma gondii argues for a red alga ancestry

Author: Steven G. Ball, David Dauvillée, Marie-Odile Soyer-Gobillard, Alain Buléon, Stanislas Tomavo, Alexandra Coppin, Luc Liénard, Yann Guérardel, Jean-Stéphane Varré, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Université des Sciences et Technologies (Lille 1) (USTL), Laboratoire d'Informatique Fondamentale de Lille (LIFL), Université de Lille, Sciences et Technologies-Institut National de Recherche en Informatique et en Automatique (Inria)-Université de Lille, Sciences Humaines et Sociales-Centre National de la Recherche Scientifique (CNRS), Modèles en biologie cellulaire et évolutive (MBCE), Observatoire océanologique de Banyuls (OOB), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Observatoire océanologique de Banyuls (OOB), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique, Centre de Recherches Agroalimentaires, Université de Lille-Centre National de la Recherche Scientifique (CNRS), and Université de Lille, Sciences et Technologies
Subjects: 0106 biological sciences, ISOAMYLASE, Chlamydomonas reinhardtii, Red algae, RHODOPHYTE, 01 natural sciences, Microbiology, Evolution, Molecular, T. GONDII, 03 medical and health sciences, Algae, Polysaccharides, parasitic diseases, Genetics, Animals, Humans, Amino Acid Sequence, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Molecular Biology, Ecology, Evolution, Behavior and Systematics, Phylogeny, 030304 developmental biology, 0303 health sciences, biology, Sequence Homology, Amino Acid, Dinoflagellate, Toxoplasma gondii, food and beverages, PLANT-LIKE METABOLISM, GLUCAN WATER DIKINASE, Glycogen Debranching Enzyme System, Crypthecodinium cohnii, Apicoplasts, EVOLUTIONARY ORIGIN, biology.organism_classification, AMYLOPECTIN, FLORIDEAN STARCH, 3. Good health, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Microscopy, Electron, Cyanidioschyzon merolae, Rhodophyta, Dinoflagellida, Crystallization, ALGUE ROUGE, Toxoplasma, 010606 plant biology & botany
Abstract: International audience; Single-celled apicomplexan parasites are known to cause major diseases in humans and animals including malaria, toxoplasmosis, and coccidiosis. The presence of apicoplasts with the remnant of a plastid-like DNA argues that these parasites evolved from photosynthetic ancestors possibly related to the dinoflagellates. Toxoplasma gondii displays amylopectin-like polymers within the cytoplasm of the dormant brain cysts. Here we report a detailed structural and comparative analysis of the Toxoplasma gondii, green alga Chlamydomonas reinhardtii, and dinoflagellate Crypthecodinium cohnii storage polysaccharides. We show Toxoplasma gondii amylopectin to be similar to the semicrystalline floridean starch accumulated by red algae. Unlike green plants or algae, the nuclear DNA sequences as well as biochemical and phylogenetic analysis argue that the Toxoplasma gondii amylopectin pathway has evolved from a totally different UDP-glucose-based metabolism similar to that of the floridean starch accumulating red alga Cyanidioschyzon merolae and, to a lesser extent, to those of glycogen storing animals or fungi. In both red algae and apicomplexan parasites, isoamylase and glucan–water dikinase sequences are proposed to explain the appearance of semicrystalline starch-like polymers. Our results have built a case for the separate evolution of semicrystalline storage polysaccharides upon acquisition of photosynthesis in eukaryotes.
Published: 2005

48. Role of the Escherichia coli glgX Gene in Glycogen Metabolism

Author: David Dauvillée, Michael S. Samuel, Lynette Rampling, Zhongyi Li, Isabelle S. Kinderf, Matthew K. Morell, Behjat Kosar-Hashemi, Steven G. Ball, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), CSIRO Plant Industry, Commonwealth Scientific and Industrial Research Organisation [Canberra] (CSIRO), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), and Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Subjects: Physiology and Metabolism, Amylopectin, medicine.disease_cause, Microbiology, Substrate Specificity, Glycogen debranching enzyme, 03 medical and health sciences, chemistry.chemical_compound, Glycogen phosphorylase, Dextrins, Escherichia coli, Glycogen branching enzyme, medicine, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Glycogen synthase, Glucans, Molecular Biology, Gene, Sequence Deletion, 030304 developmental biology, 0303 health sciences, biology, Glycogen, 030306 microbiology, Futile cycle, Genetic Complementation Test, Glycogen Debranching Enzyme System, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], chemistry, Biochemistry, biology.protein
Abstract: A role for the Escherichia coli glgX gene in bacterial glycogen synthesis and/or degradation has been inferred from the sequence homology between the glgX gene and the genes encoding isoamylase-type debranching enzymes; however, experimental evidence or definition of the role of the gene has been lacking. Construction of E. coli strains with defined deletions in the glgX gene is reported here. The results show that the GlgX gene encodes an isoamylase-type debranching enzyme with high specificity for hydrolysis of chains consisting of three or four glucose residues. This specificity ensures that GlgX does not generate an extensive futile cycle during glycogen synthesis in which chains with more than four glucose residues are transferred by the branching enzyme. Disruption of glgX leads to overproduction of glycogen containing short external chains. These results suggest that the GlgX protein is predominantly involved in glycogen catabolism by selectively debranching the polysaccharide outer chains that were previously recessed by glycogen phosphorylase.
Published: 2005

49. Starch Division and Partitioning. A Mechanism for Granule Propagation and Maintenance in the Picophytoplanktonic Green Alga Ostreococcus tauri

Author: Marie-Christine Slomianny, Fabrice Wattebled, Steven G. Ball, Alain Buléon, Conchita Ferraz, David Delvallé, Stephane Rombauts, Evelyne Derelle, Christophe D'Hulst, Hervé Moreau, Jean-Philippe Ral, Florence Corellou, Benoit Farinas, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Modèles en biologie cellulaire et évolutive (MBCE), Observatoire océanologique de Banyuls (OOB), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Institut de génétique humaine (IGH), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique, Centre de Recherches Agroalimentaires, Institut National de la Recherche Agronomique (INRA), Center for Plant Systems Biology (PSB Center), Vlaams Instituut voor Biotechnologie [Ghent, Belgique] (VIB), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Observatoire océanologique de Banyuls (OOB), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Department of Plant Systems Biology, and State University of Ghent
Subjects: 0106 biological sciences, Chloroplasts, Physiology, Starch, Molecular Sequence Data, Prasinophyceae, Chlamydomonas reinhardtii, Plant Science, Cytoplasmic Granules, 01 natural sciences, Ostreococcus tauri, Adenosine Diphosphate Glucose, 03 medical and health sciences, chemistry.chemical_compound, Starch Synthase, Chlorophyta, Genetics, Plastid, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Phylogeny, 030304 developmental biology, 0303 health sciences, Genome, biology, Cell Cycle, food and beverages, biology.organism_classification, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Chloroplast, chemistry, Biochemistry, Amylopectin, biology.protein, Starch synthase, Research Article, 010606 plant biology & botany
Abstract: Whereas Glc is stored in small-sized hydrosoluble glycogen particles in archaea, eubacteria, fungi, and animal cells, photosynthetic eukaryotes have resorted to building starch, which is composed of several distinct polysaccharide fractions packed into a highly organized semicrystalline granule. In plants, both the initiation of polysaccharide synthesis and the nucleation mechanism leading to formation of new starch granules are currently not understood. Ostreococcus tauri, a unicellular green alga of the Prasinophyceae family, defines the tiniest eukaryote with one of the smallest genomes. We show that it accumulates a single starch granule at the chloroplast center by using the same pathway as higher plants. At the time of plastid division, we observe elongation of the starch and division into two daughter structures that are partitioned in each newly formed chloroplast. These observations suggest that in this system the information required to initiate crystalline polysaccharide growth of a new granule is contained within the preexisting polysaccharide structure and the design of the plastid division machinery.
Published: 2004

50. Defining the functions of maltodextrin active enzymes in starch metabolism in the unicellular alga Chlamydomonas reinhardtii

Author: Christophe D'Hulst, Glenn R. Hicks, Steven G. Ball, Luc Liénard, Martin Steup, Fabrice Wattebled, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Plant Physiology, Institute of Biochemistry and Biology, University of Potsdam, Plant Genetics, Exelixis, Inc., Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Université de Lille-Centre National de la Recherche Scientifique (CNRS), and University of Potsdam = Universität Potsdam
Subjects: biology, Glycogen, Starch, Chlamydomonas, food and beverages, Chlamydomonas reinhardtii, biology.organism_classification, Maltodextrin, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], chemistry.chemical_compound, Glycogen phosphorylase, chemistry, Biochemistry, Amylose, Amylopectin, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], ComputingMilieux_MISCELLANEOUS, Institut für Biochemie und Biologie
Abstract: Bacterial glycogen and plant starch metabolism both require the presence of malto-oligosaccharide assimilation enzymes. In Escherichia coil maltotetraose is generated through debranching of the glycogen limit dextrin produced by glycogen phosphorylase. This maltotetraose if further metabolised through the combined action of amylomaltase (an α-1, 4 glucanotransferase) and maltodextrin phosphorylase. In the starch accumulating alga Chlamydomonas reinhardtii we show that a deficiency in D-enzyme (the plant α-1, 4 glucanotransferase) leads to a severe decrease in starch content and a modification in amylopectin structure as well as a modification in amylose content. We further show that there are 2 distinct plastidial phosphorylases in Chlamydomonas. Kinetic and genetic studies suggest these forms may be related to the maltodextrin and glycogen-type of phosphorylases from bacteria.
Published: 2003

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