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dc.rights.licenseopenen_US
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorLESBATS, Paul
dc.contributor.authorSERRAO, Erik
dc.contributor.authorMASKELL, Daniel P
dc.contributor.authorPYE, Valerie E
dc.contributor.authorO'REILLY, Nicola
dc.contributor.authorLINDEMANN, Dirk
dc.contributor.authorENGELMAN, Alan N
dc.contributor.authorCHEREPANOV, Peter
dc.date.accessioned2023-11-16T12:50:58Z
dc.date.available2023-11-16T12:50:58Z
dc.date.issued2017-05-23
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/184815
dc.description.abstractEnThe interactions between a retrovirus and host cell chromatin that underlie integration and provirus expression are poorly understood. The prototype foamy virus (PFV) structural protein GAG associates with chromosomes via a chromatin-binding sequence (CBS) located within its C-terminal region. Here, we show that the PFV CBS is essential and sufficient for a direct interaction with nucleosomes and present a crystal structure of the CBS bound to a mononucleosome. The CBS interacts with the histone octamer, engaging the H2A-H2B acidic patch in a manner similar to other acidic patch-binding proteins such as herpesvirus latency-associated nuclear antigen (LANA). Substitutions of the invariant arginine anchor residue in GAG result in global redistribution of PFV and macaque simian foamy virus (SFV) integration sites toward centromeres, dampening the resulting proviral expression without affecting the overall efficiency of integration. Our findings underscore the importance of retroviral structural proteins for integration site selection and the avoidance of genomic junkyards.
dc.language.isoENen_US
dc.subject.enHistones
dc.subject.enNucleosomes
dc.subject.enSpumavirus
dc.subject.enVirus Integration
dc.title.enStructural basis for spumavirus GAG tethering to chromatin.
dc.title.alternativeProc Natl Acad Sci U S Aen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1073/pnas.1621159114en_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologieen_US
dc.identifier.pubmed28490494en_US
bordeaux.journalProceedings of the National Academy of Sciences of the United States of Americaen_US
bordeaux.page5509-5514en_US
bordeaux.volume114en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.issue21en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcepubmed
hal.identifierhal-04289334
hal.version1
hal.date.transferred2023-11-16T12:51:01Z
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exporttrue
workflow.import.sourcepubmed
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20of%20the%20United%20States%20of%20America&rft.date=2017-05-23&rft.volume=114&rft.issue=21&rft.spage=5509-5514&rft.epage=5509-5514&rft.au=LESBATS,%20Paul&SERRAO,%20Erik&MASKELL,%20Daniel%20P&PYE,%20Valerie%20E&O'REILLY,%20Nicola&rft.genre=article


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