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1. Low phosphate activates STOP1-ALMT1 to rapidly inhibit root cell elongation

Author

Coline Balzergue, Thibault Dartevelle, Christian Godon, Edith Laugier, Claudia Meisrimler, Jean-Marie Teulon, Audrey Creff, Marie Bissler, Corinne Brouchoud, Agnès Hagège, Jens Müller, Serge Chiarenza, Hélène Javot, Noëlle Becuwe-Linka, Pascale David, Benjamin Péret, Etienne Delannoy, Marie-Christine Thibaud, Jean Armengaud, Steffen Abel, Jean-Luc Pellequer, Laurent Nussaume, and Thierry Desnos

Subjects
Science
Abstract

Low Pi availability inhibits primary root growth, but the sensory mechanisms are not known. Here the authors uncover a signalling pathway regulating Pi-mediated root growth inhibition inArabidopsis, involving the transcription factor STOP1, its direct target ALMT1, a malate channel, and ferroxidase LPR1.

Published
2017
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2. Low phosphate activates STOP1-ALMT1 to rapidly inhibit root cell elongation

Author

Jean-Marie Teulon, Edith Laugier, Jean Armengaud, Serge Chiarenza, Audrey Creff, Marie-Christine Thibaud, Benjamin Péret, Steffen Abel, Jens Daniel Müller, Agnès Hagège, Coline Balzergue, Pascale David, Thierry Desnos, Marie Bissler, Christian Godon, Noëlle Becuwe-Linka, Corinne Brouchoud, Etienne Delannoy, Thibault Dartevelle, Claudia-Nicole Meisrimler, Laurent Nussaume, Hélène Javot, Jean-Luc Pellequer, 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), Biologie végétale et microbiologie environnementale - UMR7265 (BVME), 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)), Signalisation de l'Adaptation des Végétaux à l'Environnement (SAVE), Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie structurale (IBS - UMR 5075), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), 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)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Leibniz-Institut für Pflanzenbiochemie, Equipe Développement et Plasticité du Système Racinaire (PLASTICITE), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Innovations technologiques pour la Détection et le Diagnostic (LI2D), Service de Pharmacologie et Immunoanalyse (SPI), Médicaments et Technologies pour la Santé (MTS), 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)-Médicaments et Technologies pour la Santé (MTS), CEA (APTTOX021401, APTTOX021403), ANR11-RSNR-0005,DEMETERRES, ANR-09-BLAN-0118,CHEMIGENA,Génétique d'une voie limitant la croissance racinaire d'Arabidopsis en réponse à la carence phosphatée(2009), ANR-12-ADAP-0019,RNAdapt,Les ARN non-codants dans l'adaptation de la croissance racinaire à la carence phosphate(2012), 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), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), 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), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-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)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Médicaments et Technologies pour la Santé (MTS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), ANR-11-RSNR-0005,DEMETERRES,Développement de Méthodes bio-et Eco-Technologiques pour la Remédiation Raisonnée des Effluents et des Sols en appui à une stratégie de réhabilitation agricole post-accidentelle(2011), Plant Environmental Physiology and Stress Signaling (PEPSS), Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Institut de Biosciences et Biotechnologies d'Aix-Marseille (ex-IBEB) ( BIAM ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ), Biologie végétale et microbiologie environnementale - UMR7265 ( BVME ), Centre National de la Recherche Scientifique ( CNRS ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Aix Marseille Université ( AMU ), Biochimie et Physiologie Moléculaire des Plantes ( BPMP ), Centre international d'études supérieures en sciences agronomiques ( Montpellier SupAgro ) -Institut national de la recherche agronomique [Montpellier] ( INRA Montpellier ) -Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ) -Institut national d’études supérieures agronomiques de Montpellier ( Montpellier SupAgro ), Institut de biologie structurale ( IBS - UMR 5075 ), Université Joseph Fourier - Grenoble 1 ( UJF ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Grenoble Alpes ( UGA ), Laboratoire de Biologie du Développement des Plantes ( LBDP ), Université de la Méditerranée - Aix-Marseille 2-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ), Equipe Développement et Plasticité du Système Racinaire ( PLASTICITE ), Centre international d'études supérieures en sciences agronomiques ( Montpellier SupAgro ) -Institut national de la recherche agronomique [Montpellier] ( INRA Montpellier ) -Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ) -Institut national d’études supérieures agronomiques de Montpellier ( Montpellier SupAgro ) -Centre international d'études supérieures en sciences agronomiques ( Montpellier SupAgro ) -Institut national de la recherche agronomique [Montpellier] ( INRA Montpellier ) -Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ) -Institut national d’études supérieures agronomiques de Montpellier ( Montpellier SupAgro ), Laboratoire Innovations technologiques pour la Détection et le Diagnostic ( LI2D ), Service de Pharmacologie et Immunoanalyse ( SPI ), Département Médicaments et Technologies pour la Santé ( DMTS ), Direction de Recherche Fondamentale (CEA) ( DRF (CEA) ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-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 ) -Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Département Médicaments et Technologies pour la Santé ( DMTS ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay, Biologie cellulaire et moléculaire des plantes et des bactéries ( BCMPB ), and Investissements d'avenir RSNR Demeterres

Subjects
0106 biological sciences, 0301 basic medicine, immunité cellulaire, Arabidopsis, Malates, Organic Anion Transporters, General Physics and Astronomy, Plant Roots, 01 natural sciences, chemistry.chemical_compound, Cell Wall, Gene Expression Regulation, Plant, Arabidopsis thaliana, Multidisciplinary, food and beverages, [SDV.BV.BOT]Life Sciences [q-bio]/Vegetal Biology/Botanics, Plants, Genetically Modified, Apoplast, Hedgehog signaling pathway, Cell biology, Biochemistry, Oxidoreductases, paroi cellulaire, Signal Transduction, [ SDV.BV.BOT ] Life Sciences [q-bio]/Vegetal Biology/Botanics, Science, Iron, Meristem, Cell Enlargement, Biology, capacité de croissance, Article, General Biochemistry, Genetics and Molecular Biology, Phosphates, Cell wall, 03 medical and health sciences, développement de la plante, Transcription factor, Peroxidase, phosphate, prolifération cellulaire, Arabidopsis Proteins, Cell growth, Callose, arabidopsis thaliana, élongation cellulaire, General Chemistry, biology.organism_classification, racine, 030104 developmental biology, chemistry, Transcription Factors, 010606 plant biology & botany
Abstract

Environmental cues profoundly modulate cell proliferation and cell elongation to inform and direct plant growth and development. External phosphate (Pi) limitation inhibits primary root growth in many plant species. However, the underlying Pi sensory mechanisms are unknown. Here we genetically uncouple two Pi sensing pathways in the root apex of Arabidopsis thaliana. First, the rapid inhibition of cell elongation in the transition zone is controlled by transcription factor STOP1, by its direct target, ALMT1, encoding a malate channel, and by ferroxidase LPR1, which together mediate Fe and peroxidase-dependent cell wall stiffening. Second, during the subsequent slow inhibition of cell proliferation in the apical meristem, which is mediated by LPR1-dependent, but largely STOP1–ALMT1-independent, Fe and callose accumulate in the stem cell niche, leading to meristem reduction. Our work uncovers STOP1 and ALMT1 as a signalling pathway of low Pi availability and exuded malate as an unexpected apoplastic inhibitor of root cell wall expansion., Low Pi availability inhibits primary root growth, but the sensory mechanisms are not known. Here the authors uncover a signalling pathway regulating Pi-mediated root growth inhibition in Arabidopsis, involving the transcription factor STOP1, its direct target ALMT1, a malate channel, and ferroxidase LPR1.

Published
2017

3. The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response

Author

Noëlle Becuwe, Pascal Rey, Michel B. Toledano, Dominique Rumeau, Michel Havaux, Benoît Biteau, and Marie-Bénédicte Barrault

Subjects
0106 biological sciences, chemistry.chemical_classification, 0303 health sciences, biology, Mutant, Cell Biology, Plant Science, Sulfinic acid, Reductase, biology.organism_classification, 01 natural sciences, 03 medical and health sciences, chemistry.chemical_compound, Sulfiredoxin, chemistry, Biochemistry, Genetics, Cysteine sulfinic acid, Arabidopsis thaliana, Peroxiredoxin, 030304 developmental biology, 010606 plant biology & botany, Cysteine
Abstract

The 2-cysteine peroxiredoxins (2-Cys-Prxs) are antioxidants that reduce peroxides through a thiol-based mechanism. During catalysis, these ubiquitous enzymes are occasionally inactivated by the substrate-dependent oxidation of the catalytic cysteine to the sulfinic acid (-SO2H) form, and are reactivated by reduction by sulfiredoxin (Srx), an enzyme recently identified in yeast and in mammal cells. In plants, 2-Cys-Prxs constitute the most abundant Prxs and are located in chloroplasts. Here we have characterized the unique Srx gene in Arabidopsis thaliana (AtSrx) from a functional point of view, and analyzed the phenotype of two AtSrx knockout (AtSrx-) mutant lines. AtSrx is a chloroplastic enzyme displaying sulfinic acid reductase activity, as shown by the ability of the recombinant AtSrx to reduce the overoxidized 2-Cys-Prx form in vitro, and by the accumulation of the overoxidized Prx in mutant lines lacking Srx in vivo. Furthermore, AtSrx mutants exhibit an increased tolerance to photooxidative stress generated by high light combined with low temperature. These data establish that, as in yeast and in mammals, plant 2-Cys-Prxs are subject to substrate-mediated inactivation reversed by Srx, and suggest that the 2-Cys-Prx redox status and sulfiredoxin are parts of a signaling mechanism participating in plant responses to oxidative stress.

Published
2007

4. Arabidopsis glutaredoxin S17 and its partner, the nuclear factor Y subunit C11/negative cofactor 2α, contribute to maintenance of the shoot apical meristem under long-day photoperiod

Author

Janneke Balk, Jocelyne Guilleminot-Montoya, Inga Kruse, Christophe Riondet, Sébastien Tourrette, Carsten Berndt, Noëlle Becuwe, Carlos Maria, Nicolas König, Frédéric Gaymard, Johannes Knuesting, Pascal Rey, Enrique Herrero, Nicolas Rouhier, Jean-Philippe Reichheld, Renate Scheibe, and Gemma Bellí

Subjects
0106 biological sciences, Iron-Sulfur Proteins, endocrine system, Physiology, Protein subunit, Photoperiod, Mutant, Saccharomyces cerevisiae, Meristem, Arabidopsis, Plant Science, macromolecular substances, 01 natural sciences, environment and public health, Models, Biological, 03 medical and health sciences, Oxidoreductase, Gene Expression Regulation, Plant, Genes, Reporter, Glutaredoxin, Genetics, Arabidopsis thaliana, Glutaredoxins, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, biology, Arabidopsis Proteins, fungi, food and beverages, Articles, biology.organism_classification, Plants, Genetically Modified, Recombinant Proteins, Plant Leaves, Phenotype, chemistry, Biochemistry, CCAAT-Binding Factor, Mutation, Oxidation-Reduction, Plant Shoots, 010606 plant biology & botany, Signal Transduction
Abstract

Glutaredoxins (GRXs) catalyze the reduction of protein disulfide bonds using glutathione as a reductant. Certain GRXs are able to transfer iron-sulfur clusters to other proteins. To investigate the function of Arabidopsis (Arabidopsis thaliana) GRXS17, we applied a strategy combining biochemical, genetic, and physiological approaches. GRXS17 was localized in the nucleus and cytosol, and its expression was elevated in the shoot meristems and reproductive tissues. Recombinant GRXS17 bound Fe2S2 clusters, a property likely contributing to its ability to complement the defects of a Baker’s yeast (Saccharomyces cerevisiae) strain lacking the mitochondrial GRX5. However, a grxs17 knockout Arabidopsis mutant exhibited only a minor decrease in the activities of iron-sulfur enzymes, suggesting that its primary function is as a disulfide oxidoreductase. The grxS17 plants were sensitive to high temperatures and long-day photoperiods, resulting in elongated leaves, compromised shoot apical meristem, and delayed bolting. Both environmental conditions applied simultaneously led to a growth arrest. Using affinity chromatography and split-Yellow Fluorescent Protein methods, a nuclear transcriptional regulator, the Nuclear Factor Y Subunit C11/Negative Cofactor 2α (NF-YC11/NC2α), was identified as a GRXS17 interacting partner. A mutant deficient in NF-YC11/NC2α exhibited similar phenotypes to grxs17 in response to photoperiod. Therefore, we propose that GRXS17 interacts with NF-YC11/NC2α to relay a redox signal generated by the photoperiod to maintain meristem function.

Published
2015

5. A novel thioredoxin-like protein located in the chloroplast is induced by water deficit in Solanum tuberosum L. plants

Author

Ghislaine Pruvot, Gilles Peltier, Dominique Rumeau, Noëlle Becuwe, Pascal Rey, and Françoise Eymery

Subjects
0106 biological sciences, chemistry.chemical_classification, 0303 health sciences, Immunoprecipitation, food and beverages, Cell Biology, Plant Science, Biology, 01 natural sciences, Fusion protein, 6. Clean water, Amino acid, Chloroplast, 03 medical and health sciences, Biochemistry, chemistry, 13. Climate action, Complementary DNA, Gene expression, Genetics, Protein biosynthesis, Thioredoxin, 030304 developmental biology, 010606 plant biology & botany
Abstract

Summary By analysing two-dimensional patterns of chloroplastic proteins from Solanum tuberosum, the authors observed the accumulation of a 32-kDa polypeptide in the stroma of plants subjected to water deficit. N-terminus and internal peptides of the protein, named CDSP 32 for chloroplastic drought-induced stress protein, showed no obvious homology with known sequences. Using a serum raised against the protein N-terminus, a cDNA encoding CDSP 32 was cloned by screening an expression library. The deduced mature CDSP 32 protein is 243 amino acids long and displays typical features of thioredoxins in the C-terminal region (122 residues). In particular, CDSP 32 contains a CGPC motif corresponding to a thioredoxin active site and a number of amino acids conferring thioredoxin-type structure. The CDSP 32 C-terminal region was expressed as a fusion protein in Escherichia coli and was shown to possess thioredoxin activity based on reduction assay of insulin disulfide bridges. RNA blot analysis showed that CDSP 32 transcript does not accumulate upon mild water deficit conditions corresponding to leaf relative water contents (RWC) around 85%, but high levels of CDSP 32 transcripts were observed for more severe stress conditions (RWC around 70%). In vivo labelling and immunoprecipitation revealed a substantial increase in CDSP 32 synthesis upon similar stress conditions. Rewatering of wilted plants caused decreases in both transcript and protein abundances. In tomato wild-type plants and ABAdeficient mutants, a similar accumulation of a CDSP 32related transcript was observed upon water deficit, most likely indicating no requirement for ABA in the regulation of CDSP 32 synthesis. Based on these results, it is proposed that CDSP 32 plays a role in preservation of the thiol: disulfide redox potential of chloroplastic proteins during water deficit.

Published
2002

6. PSII-S gene expression, photosynthetic activity and abundance of plastid thioredoxin-related and lipid-associated proteins during chilling stress in Solanum species differing in freezing resistance

Author

Michel Havaux, Stéphan Cuiné, Tadeusz Rorat, Noëlle Becuwe, Pascal Rey, Witold Irzykowski, Institut de Biosciences et Biotechnologies d'Aix-Marseille (ex-IBEB) (BIAM), 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), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
0106 biological sciences, Physiology, Plant Science, Biology, Photosynthesis, 01 natural sciences, Acclimatization, Energy quenching, 03 medical and health sciences, Botany, Genetics, Cold acclimation, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, Plastid, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, fungi, food and beverages, Cell Biology, General Medicine, Solanum tuberosum, biology.organism_classification, Biochemistry, Solanum, Thioredoxin, 010606 plant biology & botany
Abstract

We investigated the role of non-photochemical energy quenching (NPQ) in cold acclimation in potato. We first analyzed the expression of the PsbS gene, which encodes a PSII subunit involved in NPQ, during chilling treatment in two potato species, a cold-tolerant Solanum sogarandinum and a cold-sensitive Solanum tuberosum (cv. Cisa). In in vitro plantlets, a transient transcript accumulation was observed after 1 h in the light at room temperature in both species, and this light-induced PsbS transcript accumulation was strongly amplified at 4°C. Nuclear run-off transcription experiments indicated that this increase likely originates from a higher transcriptional activity of PsbS gene. In phytotron-grown plants, chilling treatment was shown also to result in a substantial increase in PsbS mRNA level. However, no change in protein abundance was noticed in either Solanum species. PSII photochemistry and photosynthetic electron transport were severely decreased in S. tuberosum plants at low temperature, while both activities were only slightly affected in S. sogarandinum. NPQ was substantially reduced in both species during chilling stress. These results indicate that neither PsbS nor NPQ are involved in acclimation of S. sogarandinum to low temperature. In contrast, the level of two other plastid proteins, one related to thioredoxins, CDSP32, and the other homologous to plastid lipid-associated proteins, CDSP34 (for chloroplastic drought-induced stress proteins of 32 and 34 kDa, respectively), was higher at low temperature in the cold-tolerant species. This result is discussed in relation to the potential roles of CDSPs in the protection of photosynthetic structures.

Published
2001

7. Investigation of the role of glutaredoxins and NFU proteins for the plastidial iron-sulfur cluster assembly machinary

Author

Brigitte Touraine, Pascal Rey, Maryline Lièvre, Hui-Chen Wu, Hunyao Gao, Jérémy Couturier, Tiphaine Lamant, Noëlle Becuwe, Jean-Francois Briat, Michel Havaux, Florence Vignols, Johnson, Michael K., Frédéric Gaymard, Nicolas Rouhier, Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), CEA Cadarache, Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia [USA], Interactions Arbres-Microorganismes (IAM), Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL), and Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)

Subjects
[SDV]Life Sciences [q-bio], [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2012

8. Accumulation of plastid lipid‐associated proteins (fibrillin/CDSP34) upon oxidative stress, ageing and biotic stress in Solanaceae and in response to drought in other species

Author

Nathalie Manac'h, Noëlle Becuwe, Pascal Rey, Mélanie Broin, Georg Langenkämper, Stéphan Cuiné, Marcel Kuntz, 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), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), and 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)

Subjects
0106 biological sciences, Transcriptional Activation, Time Factors, Light, Physiology, Plastoglobule, Plant Science, Fibrillins, 01 natural sciences, 03 medical and health sciences, Species Specificity, Gene Expression Regulation, Plant, Chromoplast, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, Genetically modified tomato, Plastids, Promoter Regions, Genetic, Solanaceae, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, Plant Proteins, 2. Zero hunger, 0303 health sciences, biology, Abiotic stress, fungi, Microfilament Proteins, food and beverages, Gene Expression Regulation, Developmental, Water, Biotic stress, biology.organism_classification, Plants, Genetically Modified, Adaptation, Physiological, Plant Leaves, Oxidative Stress, Biochemistry, Plant protein, RNA, Plant, Fibrillin, 010606 plant biology & botany
Abstract

Plastid lipid-associated proteins, also termed fibrillin/CDSP34 proteins, are known to accumulate in fibrillar-type chromoplasts such as those of ripening pepper fruit, and in leaf chloroplasts from Solanaceae plants under abiotic stress conditions. It is shown here that treatments generating active oxygen species (high light combined with low temperature, gamma irradiation or methyl viologen treatment) result in potato CDSP34 gene induction and protein accumulation in leaves. Using transgenic tomato plants containing the pepper fibrillin promoter, a significant increase in promoter activity in leaves subjected to biotic stress, namely bacterial infections, was observed. In WT, a higher level of the endogenous fibrillin/CDSP34 protein is also observed after infection by E. chrysanthemi strain 3739. In addition to stress-related induction, a progressive increase in the fibrillin promoter activity is noticed during ageing in various tomato photosynthetic tissues and this increase correlates with a higher abundance of the endogenous protein in WT leaves. It is proposed that a mechanism related to oxidative events plays an essential role in the regulation of fibrillin/CDSP34 genes during stress and also during development. Using a biolistic transient expression assay, the pepper fibrillin promoter is found to be active in various dicot species, but not in monocots. Further, substantially increased levels of fibrillin/ CDSP34 proteins are shown in various dicotyledonous and monocotyledonous plants in response to water deficit.

Published
2001

9. A genetic linkage map of human chromosome 20 composed entirely of microsatellite markers

Author

Noëlle Becuwe, Jamilé Hazan, Marie-Pascale Pankowiak, Jean Weissenbach, and Christopher Dubay

Subjects
Genetics, Genetic Markers, Male, Polymorphism, Genetic, Genotype, Genetic Linkage, Chromosomes, Human, Pair 20, Chromosome, Chromosome Mapping, Biology, DNA, Satellite, Polymerase Chain Reaction, Gene mapping, Genetic distance, Genetic marker, Genetic linkage, Microsatellite, Humans, Female, Chromosome 20, Repetitive Sequences, Nucleic Acid
Abstract

Twenty-six (CA)n polymorphic microsatellites were isolated from a flow-sorted chromosome 20 library. To reduce the number of sequencing gels, these microsatellites were genotyped on 15 CEPH families using a procedure derived from the multiplex sequencing technique of G. M. Church and S. Kieffer-Higgins (1988, Science 240:185-188). A primary map with a strongly supported order was constructed with 15 (CA)n markers. Regional localizations for the 11 other microsatellites were obtained with regard to the primary map. The 26 loci span approximately 160 cM. Regional localizations for a set of index markers (D20S4, D20S6, D20S16, and D20S19) and for other markers from the CEPH Public Database (D20S5, D20S15, D20S17, and D20S18) have also been determined. The total map spans a genetic distance of approximately 195 cM extending from the (CA)n marker IP20M7 on 20p to D20S19 on 20q. The density of microsatellite markers is markedly higher in the pericentromeric region, with an average distance of 3 to 4 cM between adjacent markers over a distance of 43 cM. Two-thirds of these randomly isolated microsatellites are clustered in that region between D20S5 and D20S16 representing approximately one-fourth of the linkage map. This might suggest a nonrandom distribution of (CA)n simple sequence repeats on this chromosome.

Published
1992

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