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1. The interactome of CLUH reveals its association to SPAG5 and its co-translational proximity to mitochondrial proteins

Author

Mickaële Hémono, Alexandre Haller, Johana Chicher, Anne-Marie Duchêne, Richard Patryk Ngondo, Institut de biologie moléculaire des plantes (IBMP), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Plateforme Protéomique Strasbourg - Esplanade (IBMC / CNRS FRC1589 / UNIV Strasbourg), Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC), and Malbec, Odile

Subjects
Translation, Physiology, QH301-705.5, [SDV]Life Sciences [q-bio], Cell Cycle Proteins, TurboID, Plant Science, SPAG5, General Biochemistry, Genetics and Molecular Biology, Mitochondrial Proteins, Mice, Proximity labeling, Structural Biology, Nuclear encoded mitochondrial proteins, Animals, Humans, Sciences du Vivant [q-bio]/Biologie végétale, Biology (General), BioID, Ecology, Evolution, Behavior and Systematics, Mammals, Localized translation, Cell Biology, [SDV] Life Sciences [q-bio], CLUH, RNA binding proteins, General Agricultural and Biological Sciences, Developmental Biology, Biotechnology, Research Article
Abstract

Background Mitochondria require thousands of proteins to fulfill their essential function in energy production and other fundamental biological processes. These proteins are mostly encoded by the nuclear genome, translated in the cytoplasm before being imported into the organelle. RNA binding proteins (RBPs) are central players in the regulation of this process by affecting mRNA translation, stability, or localization. CLUH is an RBP recognizing specifically mRNAs coding for mitochondrial proteins, but its precise molecular function and interacting partners remain undiscovered in mammals. Results Here we reveal for the first time CLUH interactome in mammalian cells. Using both co-IP and BioID proximity-labeling approaches, we identify novel molecular partners interacting stably or transiently with CLUH in HCT116 cells and mouse embryonic stem cells. We reveal stable RNA-independent interactions of CLUH with itself and with SPAG5 in cytosolic granular structures. More importantly, we uncover an unexpected proximity of CLUH to mitochondrial proteins and their cognate mRNAs in the cytosol. We show that this interaction occurs during the process of active translation and is dependent on CLUH TPR domain. Conclusions Overall, through the analysis of CLUH interactome, our study sheds a new light on CLUH molecular function by revealing new partners and by highlighting its link to the translation and subcellular localization of some mRNAs coding for mitochondrial proteins.

Published
2021
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2. The Esterase PfeE, the Achilles’ Heel in the Battle for Iron between Pseudomonas aeruginosa and Escherichia coli

Author

Philippe Hammann, Véronique Gasser, Laurianne Kuhn, Laurent Aussel, Isabelle J. Schalk, Thibaut Hubert, Biotechnologie et signalisation cellulaire (BSC), Université de Strasbourg (UNISTRA)-Institut de recherche de l'Ecole de biotechnologie de Strasbourg (IREBS)-Centre National de la Recherche Scientifique (CNRS), Plateforme Protéomique Strasbourg - Esplanade (IBMC / CNRS FRC1589 / UNIV Strasbourg), Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de chimie bactérienne (LCB), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut de recherche de l'Ecole de biotechnologie de Strasbourg (IREBS), and Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC)

Subjects
0301 basic medicine, Siderophore, TonB, siderophore, [SDV]Life Sciences [q-bio], 030106 microbiology, education, Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire, medicine.disease_cause, Esterase, Catalysis, outer membrane transporters, Microbiology, lcsh:Chemistry, Inorganic Chemistry, 03 medical and health sciences, chemistry.chemical_compound, Enterobactin, medicine, otorhinolaryngologic diseases, Physical and Theoretical Chemistry, lcsh:QH301-705.5, Molecular Biology, Escherichia coli, Spectroscopy, biology, Chemistry, Pseudomonas aeruginosa, co-cultures, iron uptake, Organic Chemistry, General Medicine, Periplasmic space, biology.organism_classification, Computer Science Applications, 030104 developmental biology, lcsh:Biology (General), lcsh:QD1-999, iron homeostasis, enterobactin, Bacterial outer membrane, Bacteria
Abstract

Bacteria access iron, a key nutrient, by producing siderophores or using siderophores produced by other microorganisms. The pathogen Pseudomonas aeruginosa produces two siderophores but is also able to pirate enterobactin (ENT), the siderophore produced by Escherichia coli. ENT-Fe complexes are imported across the outer membrane of P. aeruginosa by the two outer membrane transporters PfeA and PirA. Iron is released from ENT in the P. aeruginosa periplasm by hydrolysis of ENT by the esterase PfeE. We show here that pfeE gene deletion renders P. aeruginosa unable to grow in the presence of ENT because it is unable to access iron via this siderophore. Two-species co-cultures under iron-restricted conditions show that P. aeruginosa strongly represses the growth of E. coli as long it is able to produce its own siderophores. Both strains are present in similar proportions in the culture as long as the siderophore-deficient P. aeruginosa strain is able to use ENT produced by E. coli to access iron. If pfeE is deleted, E. coli has the upper hand in the culture and P. aeruginosa growth is repressed. Overall, these data show that PfeE is the Achilles’ heel of P. aeruginosa in communities with bacteria producing ENT.

Published
2021
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3. Brain adiponectin signaling controls peripheral insulin response in Drosophila

Author

Arquier, Nathalie, Bjordal, Marianne, Hammann, Philippe, Kuhn, Lauriane, Léopold, Pierre, ARQUIER, Nathalie, Theories and Approaches of Genomic Complexity (TAGC), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Biologie Valrose (IBV), 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)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Plateforme Protéomique Strasbourg - Esplanade (IBMC / CNRS FRC1589 / UNIV Strasbourg), Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC), Génétique et Biologie du Développement, Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA)-Centre National de la Recherche Scientifique (CNRS), and Institut Curie, PSL Research University, CNRS UMR3215, INSERM U934, Paris, France.

Subjects
Science, [SDV]Life Sciences [q-bio], Article, Cell Line, Animals, Genetically Modified, Hemolymph, Animals, Drosophila Proteins, Homeostasis, Insulin, Neurons, Insulin signalling, Brain, nutritional and metabolic diseases, Neuroendocrinology, Juvenile Hormones, [SDV] Life Sciences [q-bio], Drosophila melanogaster, Metabolism, Larva, Neuronal development, Receptors, Adiponectin, Energy Metabolism, hormones, hormone substitutes, and hormone antagonists, Signal Transduction
Abstract

The brain plays a key role in energy homeostasis, detecting nutrients, metabolites and circulating hormones from peripheral organs and integrating this information to control food intake and energy expenditure. Here, we show that a group of neurons in the Drosophila larval brain expresses the adiponectin receptor (AdipoR) and controls systemic growth and metabolism through insulin signaling. We identify glucose-regulated protein 78 (Grp78) as a circulating antagonist of AdipoR function produced by fat cells in response to dietary sugar. We further show that central AdipoR signaling inhibits peripheral Juvenile Hormone (JH) response, promoting insulin signaling. In conclusion, we identify a neuroendocrine axis whereby AdipoR-positive neurons control systemic insulin response., Circulating adiponectin controls sensitivity to insulin in tissues. Here, Arquier et al. show that adiponectin receptor activity in neurons of the Drosophila brain controls insulin response in peripheral tissues via juvenile hormone signaling.

Published
2021
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4. Human Dicer helicase domain recruits PKR and dsRNA binding proteins during viral infection

Author

Montavon, Thomas, Baldaccini, Morgane, Lefèvre, Mathieu, Girardi, Erika, Chane-Woon-Ming, Béatrice, Messmer, Mélanie, Hammann, Philippe, Chicher, Johana, Pfeffer, Sébastien, Institut de biologie moléculaire des plantes (IBMP), Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Architecture et Réactivité de l'ARN (ARN), Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Institut de Génomique d'Evry (IG), 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)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Plateforme Protéomique Strasbourg - Esplanade (IBMC / CNRS FRC1589 / UNIV Strasbourg), Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC), Architecture et réactivité de l'ARN (ARN), Centre National de la Recherche Scientifique (CNRS)-Université Louis Pasteur - Strasbourg I, ANR-10-IDEX-0002,UNISTRA,Par-delà les frontières, l'Université de Strasbourg(2010), European Project: 647455,H2020,ERC-2014-CoG,RegulRNA(2016), Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Université Paris-Saclay-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), and Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
enzymes and coenzymes (carbohydrates), viruses, [SDV]Life Sciences [q-bio], fungi, food and beverages
Abstract

The antiviral innate immune response mainly involves type I interferon (IFN) in mammalian cells. The contribution of the RNA silencing machinery remains to be established, but several recent studies indicate that the ribonuclease DICER can generate viral siRNAs in specific conditions. It has also been proposed that type I IFN and RNA silencing could be mutually exclusive antiviral responses. In order to decipher the implication of DICER during infection of human cells with the Sindbis virus, we determined its interactome by proteomics analysis. We show that DICER specifically interacts with several double-stranded RNA binding proteins and RNA helicases during viral infection. In particular, proteins such as DHX9, ADAR-1 and the protein kinase RNA-activated (PKR) are enriched with DICER in virus-infected cells. We demonstrate the importance of DICER helicase domain in its interaction with PKR and showed that it has functional consequences for the cellular response to viral infection.

Published
2020

5. Molecular connection between the TUTase URT1 and decapping activators

Author

Scheer, Hélène, de Almeida, Caroline, Ferrier, Emilie, Poirier, Laure, Pflieger, David, Sement, François, Koechler, Sandrine, Piermaria, Christina, Chicher, Johana, Kuhn, Lauriane, Hammann, Philippe, Zuber, Hélène, GAGLIARDI, Dominique, Institut de biologie moléculaire des plantes (IBMP), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Plateforme Protéomique Strasbourg - Esplanade (IBMC / CNRS FRC1589 / UNIV Strasbourg), Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC), ANR-15-CE12-0008,3'modRN,Modifications des extrémités 3' des ARNm par addition de nucléotides: impact sur la traduction et la dégradation des ARNm chez Arabidopsis thaliana(2015), and ANR: NetRNA,ANR-10-LABX-0036_NETRNA

Subjects
GIGYF, RNA degradation, Arabidopsis, decapping, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Uridylation, TUTase, deadenylation, DCP5
Abstract

Uridylation is a widespread modification destabilizing eukaryotic mRNAs. Yet, molecular mechanisms underlying TUTase-mediated mRNA degradation remain mostly unresolved. Here, we report that the Arabidopsis TUTase URT1 participates in a molecular network connecting several translational repressors/decapping activators including DECAPPING 5 (DCP5), the Arabidopsis ortholog of human LSM14 and yeast Scd6. A conserved Helical Leucine-rich Motif (HLM) within an intrinsically disordered region of URT1 binds to the LSm domain of DCP5. This interaction connects URT1 to additional decay factors like DDX6/Dhh1-like RNA helicases. The combination of in planta and in vitro analyses supports a model that explains how URT1 reduces the accumulation of oligo(A)-tailed mRNAs: first, by connecting decapping factors and second, because 3’ terminal uridines can intrinsically hinder deadenylation. Importantly, preventing the accumulation of excessively deadenylated mRNAs in Arabidopsis avoids the biogenesis of illegitimate siRNAs that silence endogenous mRNAs and perturb plant growth and development.

Published
2020

6. Proteomic Analysis of DNA Synthesis on a Structured DNA Template in Human Cellular Extracts: Interplay Between NHEJ and Replication‐Associated Proteins

Author

Philippe Frit, Philippe Hammann, Lajos Haracska, Agnès M. Cordonnier, Jérôme Wagner, Lauriane Kuhn, Johana Chicher, Régine Janel-Bintz, Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Institut de pharmacologie et de biologie structurale (IPBS), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Institut de génétique et biologie moléculaire et cellulaire (IGBMC), Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), CNRS FRE3211 (FRE3211), Centre National de la Recherche Scientifique (CNRS), CORDONNIER, AGNES, Biotechnologie et signalisation cellulaire (BSC), Université de Strasbourg (UNISTRA)-Institut de recherche de l'Ecole de biotechnologie de Strasbourg (IREBS)-Centre National de la Recherche Scientifique (CNRS), Plateforme Protéomique Strasbourg - Esplanade (IBMC / CNRS FRC1589 / UNIV Strasbourg), Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC), Equipe Labellisée Ligue Contre le Cancer 2018 [Toulouse], Institute of Genetics, Biological Research Center [Szeged, Hungary], Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut de recherche de l'Ecole de biotechnologie de Strasbourg (IREBS), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), and Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées

Subjects
Cell Extracts, DNA Replication, Proteomics, DNA End-Joining Repair, Proteome, Inverted repeat, [SDV]Life Sciences [q-bio], DNA-Activated Protein Kinase, Sciences du Vivant [q-bio]/Cancer, Biochemistry, Cofactor, Primer extension, DNA Ligase ATP, 03 medical and health sciences, chemistry.chemical_compound, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Ku Autoantigen, Molecular Biology, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, DNA ligase, DNA synthesis, biology, Oligonucleotide, 030302 biochemistry & molecular biology, Mutagenesis, Nuclear Proteins, DNA-PK complex, DNA, Cell biology, DNA-Binding Proteins, [SDV] Life Sciences [q-bio], short inverted repeat, chemistry, biology.protein, Protein Binding
Abstract

International audience; It is established that short inverted repeats trigger base substitution mutagenesis in human cells. However, how the replication machinery deals with structured DNA is unknown. It has been previously reported that in human cell-free extracts, DNA primer extension using a structured single-stranded template is transiently blocked at DNA hairpins. Here, the proteomic analysis of proteins bound to the DNA template is reported and evidence that the DNA-PK complex (DNA-PKcs and the Ku heterodimer) recognizes, and is activated by, structured single-stranded DNA is provided. Hijacking the DNA-PK complex by double-stranded oligonucleotides results in a large removal of the pausing sites and an elevated DNA extension efficiency. Conversely, DNA-PKcs inhibition results in its stabilization on the template, along with other proteins acting downstream in the Non-Homologous End-Joining (NHEJ) pathway, especially the XRCC4-DNA ligase 4 complex and the cofactor PAXX. Retention of NHEJ factors to the DNA in the absence of DNA-PKcs activity correlates with additional halts of primer extension, suggesting that these proteins hinder the progression of the DNA synthesis at these sites. Overall these results raise the possibility that, upon binding to hairpins formed onto ssDNA during fork progression, the DNA-PK complex interferes with replication fork dynamics in vivo.

Published
2020
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7. The IRES5′UTR of the dicistrovirus cricket paralysis virus is a type III IRES containing an essential pseudoknot structure

Author

Gross, Lauriane, Vicens, Quentin, Einhorn, Evelyne, Noireterre, Audrey, Schaeffer, Laure, Kuhn, Lauriane, Imler, Jean-Luc, Eriani, Gilbert, Meignin, Carine, Martin, Franck, Architecture et Réactivité de l'ARN (ARN), Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Modèles Insectes de l'Immunité Innée (M3I), Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Plateforme Protéomique Strasbourg - Esplanade (IBMC / CNRS FRC1589 / UNIV Strasbourg), Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC), Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, Investissement d’Avenir program [NetRNA ANR-10-LABX-36, ANR ANR-11-SVSE802501]. Funding for open access charge: Centre National de la Recherche Scientifique., MATHELIN, Sandra, and Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Base Sequence, Cell-Free System, [SDV]Life Sciences [q-bio], fungi, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Internal Ribosome Entry Sites, [SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Cell Line, [SDV] Life Sciences [q-bio], Gryllidae, Open Reading Frames, Viral Proteins, Drosophila melanogaster, Protein Biosynthesis, Host-Pathogen Interactions, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Dicistroviridae, Animals, Nucleic Acid Conformation, RNA, Viral, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, 5' Untranslated Regions, Molecular Biology, Ribosomes
Abstract

International audience; Cricket paralysis virus (CrPV) is a dicistrovirus. Its positive-sense single-stranded RNA genome contains two internal ribosomal entry sites (IRESs). The 5' untranslated region (5'UTR) IRES5'UTR mediates translation of non-structural proteins encoded by ORF1 whereas the well-known intergenic region (IGR) IRESIGR is required for translation of structural proteins from open reading frame 2 in the late phase of infection. Concerted action of both IRES is essential for host translation shut-off and viral translation. IRESIGR has been extensively studied, in contrast the IRES5'UTR remains largely unexplored. Here, we define the minimal IRES element required for efficient translation initiation in drosophila S2 cell-free extracts. We show that IRES5'UTR promotes direct recruitment of the ribosome on the cognate viral AUG start codon without any scanning step, using a Hepatitis-C virus-related translation initiation mechanism. Mass spectrometry analysis revealed that IRES5'UTR recruits eukaryotic initiation factor 3, confirming that it belongs to type III class of IRES elements. Using Selective 2'-hydroxyl acylation analyzed by primer extension and DMS probing, we established a secondary structure model of 5'UTR and of the minimal IRES5'UTR. The IRES5'UTR contains a pseudoknot structure that is essential for proper folding and ribosome recruitment. Overall, our results pave the way for studies addressing the synergy and interplay between the two IRES from CrPV.

Published
2017
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8. The RNA targetome of Staphylococcus aureus non-coding RNA RsaA: impact on cell surface properties and defense mechanisms

Author

Tomasini, Arnaud, Moreau, Karen, Chicher, Johana, Geissmann, Thomas, Vandenesch, François, Romby, Pascale, Marzi, Stefano, Caldelari, Isabelle, Architecture et Réactivité de l'ARN (ARN), Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Pathogénie des Staphylocoques – Staphylococcal Pathogenesis (StaPath), Centre International de Recherche en Infectiologie - UMR (CIRI), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Plateforme Protéomique Strasbourg - Esplanade (IBMC / CNRS FRC1589 / UNIV Strasbourg), Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC), Centre International de Recherche en Infectiologie (CIRI), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), and ANR-16-CE11-0007,RIBOSTAPH,La traduction et son contrôle chez Staphylococcus aureus: conséquences sur la virulence et la réponse aux stress(2016)

Subjects
Staphylococcus aureus, RNA, Untranslated, Binding Sites, Base Sequence, Proteome, Messenger, Bacterial, Untranslated, Membrane Proteins, Gene Expression Regulation, Bacterial, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, RNA, Bacterial, Bacterial Proteins, Gene Expression Regulation, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, RNA, [SDV.IMM]Life Sciences [q-bio]/Immunology, RNA Interference, RNA, Messenger, Transcriptome
Abstract

International audience; The virulon of Staphyloccocus aureus is controlled by intricate connections between transcriptional and post-transcriptional regulators including proteins and small non-coding RNAs (sRNAs). Many of the sRNAs regulate gene expression through base-pairings with mRNAs. However, characterization of the direct sRNA targets in Gram-positive bacteria remained a difficult challenge. Here, we have applied and adapted the MS2-affinity purification approach coupled to RNA sequencing (MAPS) to determine the targetome of RsaA sRNA of S. aureus, known to repress the synthesis of the transcriptional regulator MgrA. Several mRNAs were enriched with RsaA expanding its regulatory network. Besides mgrA, several of these mRNAs encode a family of SsaA-like enzymes involved in peptidoglycan metabolism and the secreted anti-inflammatory FLIPr protein. Using a combination of in vivo and in vitro approaches, these mRNAs were validated as direct RsaA targets. Quantitative differential proteomics of wild-type and mutant strains corroborated the MAPS results. Additionally, it revealed that RsaA indirectly activated the synthesis of surface proteins supporting previous data that RsaA stimulated biofilm formation and favoured chronic infections. All together, this study shows that MAPS could also be easily applied in Gram-positive bacteria for identification of sRNA targetome.

Published
2017
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9. Advanced Antibody-Drug Conjugate Structural Characterization by Sheathless Capillary Electrophoresis-Tandem Mass Spectrometry Using Complementary Approaches

Author

Said, Nassur, Giorgetti, Jérémie, Kuhn, Lauriane, Beck, Alain, Leize-Wagner, Emmanuelle, Gahoual, Rabah, Francois, Yannis-Nicolas, Chimie de la matière complexe (CMC), Université de Strasbourg (UNISTRA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Plateforme Protéomique Strasbourg - Esplanade (IBMC / CNRS FRC1589 / UNIV Strasbourg), Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC), Centre d'Immunologie Pierre Fabre (CIPF), PIERRE FABRE, and dhotel, helene

Subjects
[SDV] Life Sciences [q-bio], [SDV.SP] Life Sciences [q-bio]/Pharmaceutical sciences, [SDV.GEN]Life Sciences [q-bio]/Genetics, [SDV.BIO]Life Sciences [q-bio]/Biotechnology, [SDV]Life Sciences [q-bio], [SDV.GEN] Life Sciences [q-bio]/Genetics, [SDV.SP]Life Sciences [q-bio]/Pharmaceutical sciences, ComputingMilieux_MISCELLANEOUS, [SDV.BIO] Life Sciences [q-bio]/Biotechnology
Abstract

International audience

Published
2017

10. eIF3 Peripheral Subunits Rearrangement after mRNA Binding and Start-Codon Recognition

Author

Adeline Renaud, A. Myasnikov, Lauriane Kuhn, Angelita Simonetti, Yaser Hashem, Jailson Brito Querido, Eder Mancera-Martínez, MATHELIN, Sandra, Initiative d'excellence - Par-delà les frontières, l'Université de Strasbourg - - UNISTRA2010 - ANR-10-IDEX-0002 - IDEX - VALID, Architecture et Réactivité de l'ARN (ARN), Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Plateforme Protéomique Strasbourg - Esplanade (IBMC / CNRS FRC1589 / UNIV Strasbourg), Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC), This work was supported by the ANR grant @RAction program ‘‘ANR CryoEM80S’’ and the LABEX: ANR-10-LABX-0036_NETRNA and benefits from funding from the state managed by the French National Research Agency as part of the Investments for the Future program (to Y.H.)., ANR-10-IDEX-0002,UNISTRA,Par-delà les frontières, l'Université de Strasbourg(2010), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)

Subjects
Models, Molecular, 0301 basic medicine, MESH: Eukaryotic Initiation Factor-3, Five prime untranslated region, MESH: Eukaryotic Initiation Factor-2, Protein Conformation, Eukaryotic Initiation Factor-3, MESH: Codon, Initiator, [SDV]Life Sciences [q-bio], Eukaryotic Initiation Factor-2, Eukaryotic Initiation Factor-1, Codon, Initiator, MESH: Rabbits, beta-Globins, [SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, MESH: Structure-Activity Relationship, MESH: Protein Conformation, RNA, Transfer, Eukaryotic initiation factor, MESH: Animals, MESH: Protein Subunits, [SDV] Life Sciences [q-bio], MESH: Nucleic Acid Conformation, ribosome, MESH: Protein Biosynthesis, Transfer RNA, Rabbits, eIF3, MESH: Eukaryotic Initiation Factor-1, MESH: Models, Molecular, Protein Binding, eukaryotic translation initiation, Biology, Structure-Activity Relationship, 03 medical and health sciences, Eukaryotic translation, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Animals, Humans, MESH: Protein Binding, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, RNA, Messenger, Molecular Biology, eIF3 peripheral subunits, MESH: RNA, Messenger, Binding Sites, MESH: Humans, MESH: beta-Globins, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Cell Biology, MESH: Multiprotein Complexes, MESH: RNA, Transfer, Molecular biology, Ribosomal binding site, Protein Subunits, Internal ribosome entry site, 030104 developmental biology, MESH: Binding Sites, Multiprotein Complexes, Protein Biosynthesis, eIF4A, Nucleic Acid Conformation, cryo-EM, Ribosomes, MESH: Ribosomes
Abstract

International audience; mRNA translation initiation in eukaryotes requires the cooperation of a dozen eukaryotic initiation factors (eIFs) forming several complexes, which leads to mRNA attachment to the small ribosomal 40S subunit, mRNA scanning for start codon, and accommodation of initiator tRNA at the 40S P site. eIF3, composed of 13 subunits, 8 core (a, c, e, f, h, l, k, and m) and 5 peripheral (b, d, g, i, and j), plays a central role during this process. Here we report a cryo-electron microscopy structure of a mammalian 48S initiation complex at 5.8 Å resolution. It shows the relocation of subunits eIF3i and eIF3g to the 40S intersubunit face on the GTPase binding site, at a late stage in initiation. On the basis of a previous study, we demonstrate the relocation of eIF3b to the 40S intersubunit face, binding below the eIF2-Met-tRNAi(Met) ternary complex upon mRNA attachment. Our analysis reveals the deep rearrangement of eIF3 and unravels the molecular mechanism underlying eIF3 function in mRNA scanning and timing of ribosomal subunit joining.

Published
2016
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11. Helix-Forming Oligoureas: Temperature-Dependent NMR, Structure Determination, and Circular Dichroism of a Nonamer with Functionalized Side Chains

Author

Didier Rognan, Michel Marraud, Gilles Guichard, Christine Hemmerlin, Jean-Paul Briand, Vincent Semetey, Roland Graff, and Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC)

Subjects
Circular dichroism, Stereochemistry, Organic Chemistry, Biochemistry, Oligomer, Catalysis, Inorganic Chemistry, chemistry.chemical_compound, Monomer, chemistry, Drug Discovery, Pyridine, Side chain, [CHIM]Chemical Sciences, Moiety, Physical and Theoretical Chemistry, Protein secondary structure, ComputingMilieux_MISCELLANEOUS, Cotton effect
Abstract

To further investigate the degree of structural homology between γ-peptides A and N,N′-linked oligoureas B, we prepared oligourea nonamer 2 containing Ala, Val, Leu, Phe, Tyr and Lys side chains. Oligomer 2 was synthesized on solid support from activated monomers, i.e., from enantiomerically pure succinimidyl {2-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}ethyl}carbamates 3a–f that are further substituted at C(2) of the ethyl moiety. These precursors were conveniently prepared from N-Fmoc-protected β3-amino acids with corresponding side chains. Detailed NMR studies (DQF-COSY, TOCSY, and ROESY) in (D5)pyridine revealed that 2 adopts a regular (P)-2.5 helical secondary structure very similar to that previously determined for oligourea heptamer 1 and closely related to the (P)-2.614 helix of γ-peptides. Temperature-dependent NMR further demonstrated the conformational homogeneity and remarkable stability of the structure of 2 in pyridine. The CD spectrum of 2 (0.2 mM) was recorded in MeOH with the aim to gain more information about the conformation of oligoureas. In contrast to 2.6-helical γ-peptides, which display only a weak or no Cotton effect, oligourea 2 exhibits an intense positive Cotton effect at ca. 203 nm ([Θ]=+373000 deg cm2 dmol−1) that decreases only slowly upon increasing the temperature.

Published
2002
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12. Unexpected Stability of the Urea cis−trans Isomer in Urea-Containing Model Pseudopeptides

Author

Claude Didierjean, Arnaud-Pierre Schaffner, Jean-Paul Briand, Vincent Semetey, Gilles Guichard, Michel Marraud, André Aubry, Christine Hemmerlin, Ana Gimenez Giner, and Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC)

Subjects
Stereochemistry, Peptide, 010402 general chemistry, 01 natural sciences, Biochemistry, Turn (biochemistry), Crystal, chemistry.chemical_compound, Isomerism, [CHIM]Chemical Sciences, Urea, Moiety, Physical and Theoretical Chemistry, ComputingMilieux_MISCELLANEOUS, chemistry.chemical_classification, 010405 organic chemistry, Chemistry, Hydrogen bond, Organic Chemistry, 3. Good health, 0104 chemical sciences, Models, Chemical, Intramolecular force, Peptides, Cis–trans isomerism
Abstract

In contrast to the situation observed in the crystal state, the urea moiety in N-Boc-N'-carbamoyl-gem-diaminoalkyl derivatives (single-residue ureidopeptides) 1-4 exclusively assumes a cis-trans conformation in solution. When R(3) = H, the resulting structure can be further stabilized by an intramolecular hydrogen bond that closes an eight-membered pseudocycle. The root-mean-square deviation calculated for heavy atoms between a peptide gamma-turn and the folded conformation that we propose to call urea turn is 0.60 A. [structure: see text]

Published
2001
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13. Effective Preparation of O-Succinimidyl-2- (tert-butoxycarbonylamino)ethylcarbamate Derivatives from β-Amino Acids. Application to the Synthesis of Urea-Containing Pseudopeptides and Oligoureas

Author

C. Didierjean, Jean-Paul Briand, Gilles Guichard, Vincent Semetey, Marc Rodriguez, André Aubry, and Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC)

Subjects
chemistry.chemical_classification, 010405 organic chemistry, Chemistry, Organic Chemistry, 010402 general chemistry, 01 natural sciences, 3. Good health, 0104 chemical sciences, Amino acid, chemistry.chemical_compound, Urea, [CHIM]Chemical Sciences, Organic chemistry, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
1999
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14. Solid-phase synthesis of N,N′-unsymmetrically substituted ureas: application to the synthesis of carbaza peptides

Author

Pascal Dalbon, Jean-Paul Briand, David Limal, Michel Jolivet, Vincent Semetey, and Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC)

Subjects
chemistry.chemical_classification, Triphosgene, 010405 organic chemistry, Organic Chemistry, Peptide, 010402 general chemistry, 01 natural sciences, Biochemistry, Combinatorial chemistry, 0104 chemical sciences, chemistry.chemical_compound, Solid-phase synthesis, chemistry, Reagent, Drug Discovery, Urea, [CHIM]Chemical Sciences, Moiety, ComputingMilieux_MISCELLANEOUS
Abstract

The synthesis of Boc- or Fmoc-monoprotected propylenediamine derivatives is reported starting from N-protected α-amino acids. The introduction of these building blocks on solid support via the formation of a urea moiety leads to a new pseudopeptide family (CαCH2CH2Nα(R)CONHCα). Two carbonylating reagents, i.e N,N′-carbonyldiimidazole and triphosgene, as well as different coupling procedures, have been tested to optimize the Boc and Fmoc solid-phase synthesis of a model peptide incorporating this isosteric replacement.

Published
1999
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15. Chromatin remodeling as a mechanism for circadian prolactin transcription: rhythmic NONO and SFPQ recruitment to HLTF

Author

Jean-Louis Franc, Lauriane Kuhn, Maya Belghazi, Anne-Marie François-Bellan, Jérôme Garin, Fabienne Guillaumond, Séverine Guillen, Bénédicte Boyer, Denis Becquet, Olivier Bosler, Institut des Sciences Moléculaires de Marseille (ISM2), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Centre de recherche en neurobiologie - neurophysiologie de Marseille (CRN2M), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Plateforme Protéomique Strasbourg - Esplanade (IBMC / CNRS FRC1589 / UNIV Strasbourg), Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire d'étude de la dynamique des protéomes (LEDyP), Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-École Centrale de Marseille (ECM)-Institut de Chimie du CNRS (INC), Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC), Centre National de la Recherche Scientifique (CNRS)-École Centrale de Marseille (ECM)-Aix Marseille Université (AMU), Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Plateforme Protéomique [Marseille], Institut de Microbiologie de la Méditerranée (IMM), and Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)

Subjects
medicine.medical_specialty, endocrine system, Transcription, Genetic, Response element, Biology, Transfection, Models, Biological, Biochemistry, Chromatin remodeling, Cell Line, E-Box Elements, Histones, 03 medical and health sciences, 0302 clinical medicine, Helicase-Like Transcription Factor, Internal medicine, Genetics, medicine, Animals, CLOCK Proteins, RNA, Messenger, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], PTB-Associated Splicing Factor, Promoter Regions, Genetic, HLTF, Molecular Biology, Transcription factor, 030304 developmental biology, 0303 health sciences, Binding Sites, Base Sequence, Circadian Rhythm Signaling Peptides and Proteins, RNA-Binding Proteins, Paraspeckle, Chromatin Assembly and Disassembly, Circadian Rhythm, Prolactin, Rats, Chromatin, Cell biology, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Endocrinology, Transcription Factor Pit-1, 030217 neurology & neurosurgery, hormones, hormone substitutes, and hormone antagonists, Transcription Factors, Biotechnology
Abstract

International audience; Most clock-controlled genes (CCGs) lack the specific E-box response element necessary for direct circadian regulation. This is the case for the prolactin (Prl) gene, the expression of which oscillates in individual lactotrope pituitary cells. To characterize the processes underlying this oscillation, we used a lactotrope cell line (GH4C1 cells). In these cells, Prl gene expression fluctuated significantly during 24 h (P=0.0418). Circadian Prl transcription depended on an interaction between the pituitary-specific transcription factor, PIT-1, and the helicase-like transcription factor (HLTF), a SWI/SNF chromatin remodeler, shown here to bind the Prl promoter on an E-box that differs from the specific E-box preferentially bound by clock proteins. Circadian Prl transcription was further accompanied by marked daily chromatin transitions. While neither HLTF nor PIT-1 was rhythmically expressed, NONO and SFPQ, identified as HLTF-associated proteins by mass spectrometry, displayed a circadian pattern and bound rhythmically to the Prl promoter. Furthermore, NONO and SFPQ were functionally involved in circadian Prl transcription since overexpression of both proteins greatly reduced Prl promoter activity (P

Published
2011
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16. Stable Helical Secondary Structure in Short-Chain N,N′-Linked Oligoureas Bearing Proteinogenic Side Chains Access to both the Bruker ARX 500 facilities of the Service Commun de RMN (Faculté de Chimie, Strasbourg) and the Bruker DRX 600 NMR facilities of the Service Commun de Biophysicochimie des Interactions Moléculaires (Université Henri Poincaré, Nancy I) were deeply appreciated

Author

Gilles Guichard, Jean-Paul Briand, Christine Hemmerlin, Michel Marraud, Didier Rognan, Roland Graff, Vincent Semetey, and Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC)

Subjects
Molecular model, Hydrogen bond, Chemistry, Peptidomimetic, Stereochemistry, General Chemistry, General Medicine, Nuclear magnetic resonance spectroscopy, Catalysis, chemistry.chemical_compound, Chain (algebraic topology), Side chain, Urea, [CHIM]Chemical Sciences, Protein secondary structure, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2002
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17. ( S )- O -Succinimidyl N -[2-( tert -butoxycarbonylamino)propyl]carbamate

Author

André Aubry, Valeria Menschise, Gilles Guichard, Vincent Semetey, Jean-Paul Briand, Claude Didierjean, and Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC)

Subjects
Carbamate, 010405 organic chemistry, Hydrogen bond, Chemistry, medicine.medical_treatment, Intermolecular force, Tert-butoxy, General Chemistry, Dihedral angle, 010402 general chemistry, Condensed Matter Physics, 01 natural sciences, Medicinal chemistry, 0104 chemical sciences, 3. Good health, Crystal, medicine, [CHIM]Chemical Sciences, General Materials Science, ComputingMilieux_MISCELLANEOUS
Abstract

The mol­ecule of activated carbamate, (S)-2,5-dioxopyrrolidin-1-yl N-[2-(tert-butoxy­carbonyl­amino)­propyl]­carbamate, tBuOCONHCH(Me)CH2NHCOONC4H4O2 or C13H21N3O6, pre­pared from N-Boc-β3HAla-OH, assumes a folded conformation with the N—C—C—N torsion angle equal to 55.9 (3)°. Both N—H groups are involved in intermolecular hydrogen bonds, forming infinite chains in the crystal.

Published
2001
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18. Early detection of cacao swollen shoot virus using the polymerase chain reaction

Author

Emmanuel Jacquot, Pierre Yot, Emmanuelle Muller, ProdInra, Migration, Montpellier Cirad, Institut National de la Recherche Agronomique (INRA), and Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC)

Subjects
0106 biological sciences, Identification, 01 natural sciences, Virus, law.invention, 03 medical and health sciences, law, Virology, Theobroma cacao, Diagnostic précoce, Badnavirus, Polymerase chain reaction, 030304 developmental biology, H20 - Maladies des plantes, Plant Diseases, [SDV.MP.VIR] Life Sciences [q-bio]/Microbiology and Parasitology/Virology, 0303 health sciences, Cacao, biology, Inoculation, Reverse Transcriptase Polymerase Chain Reaction, fungi, food and beverages, Virus des végétaux, BIOLOGIE MOLECULAIRE, biology.organism_classification, Molecular biology, CSSV, 3. Good health, Plant Leaves, PCR, Shoot, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, DNA, Viral, Nucleic acid, Caulimoviridae, Cacao swollen-shoot virus, 010606 plant biology & botany
Abstract

A polymerase chain reaction assay was developed which allows early detection of cacao swollen shoot virus (CSSV) in DNA extracts from cacao plantlets agroinoculated with the Togolese isolate Agou 1. The primers used were derived from badnavirus conserved sequences and nucleic acid was extracted with the Plant DNeasy® extraction kit (Qiagen). CSSV genome was detectable between 6 and 20 days after inoculation. The first leaf symptoms appeared after 4 weeks and the first shoot swelling symptoms after 8 weeks.

Published
2001

19. Solid phase synthesis of oligoureas using O-succinimidyl-(9H-fluoren-9-ylmethoxycarbonylamino)ethylcarbamate derivatives as activated monomers

Author

Marc Rodriguez, Jean-Paul Briand, Vincent Semetey, Gilles Guichard, and Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC)

Subjects
chemistry.chemical_classification, 010405 organic chemistry, Chemistry, Organic Chemistry, 010402 general chemistry, 01 natural sciences, Biochemistry, Isocyanate, 0104 chemical sciences, Amino acid, chemistry.chemical_compound, Monomer, Solid-phase synthesis, Drug Discovery, Organic chemistry, [CHIM]Chemical Sciences, Curtius rearrangement, ComputingMilieux_MISCELLANEOUS
Abstract

An efficient stepwise synthesis of oligoureas (up to the nonamer) on solid support using O -succinimidyl-(9 H -fluoren-9-ylmethoxycarbonylamino)ethylcarbamate derivatives as activated monomers is described. These building blocks were readily prepared starting from N -Fmoc-protected β 3 -amino acids via Curtius rearrangement of the corresponding acyl azides and treatment of the resulting isocyanate with N -hydroxysuccinimide.

Published
2000
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20. Alfalfa Mosaic Virus isolated from Buddleia davidii compared with other strains

Author

WALTER, Bernard, Kuszala, J., Ravelonandro, Michel, Pinck, L., ProdInra, Migration, Station de recherches grandes cultures : Laboratoire de zoologie, Institut National de la Recherche Agronomique (INRA), and Institut de Biologie Moléculaire et Cellulaire [Strasbourg] (IBMC)

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

International audience

Published
1985

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