The invariant arginine within the chromatin-binding motif regulates both nucleolar localization and chromatin binding of Foamy virus Gag
| Autor: | Paris, Joris, Tobaly-Tapiero, Joëlle, Giron, Marie-Lou, Burlaud-Gaillard, Julien, Buseyne, Florence, Roingeard, Philippe, Lesage, Pascale, Zamborlini, Alessia, Saïb, Ali |
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| Přispěvatelé: | Pathologie cellulaire : aspects moléculaires et viraux / Pathologie et Virologie Moléculaire, Institut Universitaire d'Hématologie (IUH), Université Paris Diderot - Paris 7 (UPD7)-Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Groupe Hospitalier Saint Louis - Lariboisière - Fernand Widal [Paris], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS), Plateforme IBISA de Microscopie Electronique [CHRU de Tours] (UNIV Tours), Centre Hospitalier Régional Universitaire de Tours (CHRU Tours)-Université de Tours (UT), Morphogénèse et antigénicité du VIH et du virus des Hépatites (MAVIVH - U1259 Inserm - CHRU Tours ), Centre Hospitalier Régional Universitaire de Tours (CHRU Tours)-Université de Tours (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM), Epidémiologie et Physiopathologie des Virus Oncogènes (EPVO (UMR_3569 / U-Pasteur_3)), Institut Pasteur [Paris] (IP)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), This study was supported by CNRS, INSERM, Université Paris Diderot Sorbonne Paris Cité, CNAM and ANR (ANR-12-BSV3-0016 to AS, ANR-15-CE15-0008 to AS and FB)., We thank Axel Rethwilm and Dirk Lindemann for FV reagents, Mark Bedford for GFP-PRMTs plasmids, Christelle Doliger, Sophie Duchez and Niclas Setterblad at the Imaging, Cell selection and Genomics Department of the Institut Universitaire d’Hématologie for confocal microscopy, Claudine Pique for critical reading of the manuscript., ANR-12-BSV3-0016,PTPs,Le rôle de l'exportation et de la maturation d'ARN messagers dans la production des produits pionniers de traduction (PTPs) dans la voie du CMH de la classe I.(2012), ANR-15-CE15-0008,REEMFOAMY,L'infection humaine par les virus foamy simiens zoonotiques : rôle des facteurs virologiques et immunologiques dans la restrcition de l'emergence virale(2015), Buseyne, Florence, BLANC - Le rôle de l'exportation et de la maturation d'ARN messagers dans la production des produits pionniers de traduction (PTPs) dans la voie du CMH de la classe I. - - PTPs2012 - ANR-12-BSV3-0016 - BLANC - VALID, L'infection humaine par les virus foamy simiens zoonotiques : rôle des facteurs virologiques et immunologiques dans la restrcition de l'emergence virale - - REEMFOAMY2015 - ANR-15-CE15-0008 - AAPG2015 - VALID, Centre Hospitalier Régional Universitaire de Tours (CHRU TOURS)-Université de Tours, Université de Tours-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre Hospitalier Régional Universitaire de Tours (CHRU TOURS), Institut Pasteur [Paris]-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Institut Pasteur [Paris] |
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
Protein-Arginine N-Methyltransferases
viruses PRMT MESH: Protein-Arginine N-Methyltransferases Amino Acid Motifs Nuclear Localization Signals MESH: Nuclear Localization Signals MESH: Amino Acid Sequence MESH: Amino Acid Motifs [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases MESH: Evolution Molecular [SDV.MP.VIR] Life Sciences [q-bio]/Microbiology and Parasitology/Virology [SDV.MHEP.ME] Life Sciences [q-bio]/Human health and pathology/Emerging diseases Gag [SDV.MHEP.ME]Life Sciences [q-bio]/Human health and pathology/Emerging diseases MESH: Arginine Chromatin Nuclear trafficking Protein Transport [SDV.IMM.IA]Life Sciences [q-bio]/Immunology/Adaptive immunology MESH: Repressor Proteins MESH: Gene Products gag [SDV.IMM.IA] Life Sciences [q-bio]/Immunology/Adaptive immunology MESH: Retroviridae Infections [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology [SDV.MHEP.MI] Life Sciences [q-bio]/Human health and pathology/Infectious diseases Foamy virus Post-translational modification Chromatin-binding Protein Binding lcsh:Immunologic diseases. Allergy MESH: Cell Nucleus MESH: Protein Transport Gene Products gag Arginine Methylation MESH: Chromatin Evolution Molecular [SDV.MHEP.PED] Life Sciences [q-bio]/Human health and pathology/Pediatrics MESH: Protein Binding Humans Protein Interaction Domains and Motifs Amino Acid Sequence Cell Nucleus MESH: Protein Interaction Domains and Motifs [SDV.MHEP.PED]Life Sciences [q-bio]/Human health and pathology/Pediatrics MESH: Humans Research Nucleolus Repressor Proteins MESH: Protein Processing Post-Translational MESH: Spumavirus Spumavirus lcsh:RC581-607 Protein Processing Post-Translational Retroviridae Infections |
| Zdroj: | Retrovirology Retrovirology, 2018, 15 (1), pp.48. ⟨10.1186/s12977-018-0428-z⟩ Retrovirology, BioMed Central, 2018, 15 (1), pp.48. ⟨10.1186/s12977-018-0428-z⟩ Retrovirology, Vol 15, Iss 1, Pp 1-12 (2018) |
| ISSN: | 1742-4690 |
| Popis: | Background Nuclear localization of Gag is a property shared by many retroviruses and retrotransposons. The importance of this stage for retroviral replication is still unknown, but studies on the Rous Sarcoma virus indicate that Gag might select the viral RNA genome for packaging in the nucleus. In the case of Foamy viruses, genome encapsidation is mediated by Gag C-terminal domain (CTD), which harbors three clusters of glycine and arginine residues named GR boxes (GRI-III). In this study we investigated how PFV Gag subnuclear distribution might be regulated. Results We show that the isolated GRI and GRIII boxes act as nucleolar localization signals. In contrast, both the entire Gag CTD and the isolated GRII box, which contains the chromatin-binding motif, target the nucleolus exclusively upon mutation of the evolutionary conserved arginine residue at position 540 (R540), which is a key determinant of FV Gag chromatin tethering. We also provide evidence that Gag localizes in the nucleolus during FV replication and uncovered that the viral protein interacts with and is methylated by Protein Arginine Methyltransferase 1 (PRMT1) in a manner that depends on the R540 residue. Finally, we show that PRMT1 depletion by RNA interference induces the concentration of Gag C-terminus in nucleoli. Conclusion Altogether, our findings suggest that methylation by PRMT1 might finely tune the subnuclear distribution of Gag depending on the stage of the FV replication cycle. The role of this step for viral replication remains an open question. Electronic supplementary material The online version of this article (10.1186/s12977-018-0428-z) contains supplementary material, which is available to authorized users. |
| Databáze: | OpenAIRE |
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