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dc.rights.licenseopenen_US
dc.contributor.authorCANTARELLA, Simona
dc.contributor.authorVEZZOLI, Marco
dc.contributor.authorCARNEVALI, Davide
dc.contributor.authorMORSELLI, Marco
dc.contributor.authorZEMKE, Nathan R
dc.contributor.authorMONTANINI, Barbara
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorDAUSSY, Coralie F
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorWODRICH, Harald
hal.structure.identifierBoRdeaux Institute in onCology [Inserm U1312 - BRIC]
dc.contributor.authorTEICHMANN, Martin
IDREF: 120052652
dc.contributor.authorPELLEGRINI, Matteo
dc.contributor.authorBERK, Arnold J
dc.contributor.authorDIECI, Giorgio
dc.contributor.authorFERRARI, Roberto
dc.date.accessioned2024-09-30T09:22:19Z
dc.date.available2024-09-30T09:22:19Z
dc.date.issued2024-09-09
dc.identifier.issn1362-4962en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/202012
dc.description.abstractEnAlu retrotransposons, which form the largest family of mobile DNA elements in the human genome, have recently come to attention as a potential source of regulatory novelties, most notably by participating in enhancer function. Even though Alu transcription by RNA polymerase III is subjected to tight epigenetic silencing, their expression has long been known to increase in response to various types of stress, including viral infection. Here we show that, in primary human fibroblasts, adenovirus small e1a triggered derepression of hundreds of individual Alus by promoting TFIIIB recruitment by Alu-bound TFIIIC. Epigenome profiling revealed an e1a-induced decrease of H3K27 acetylation and increase of H3K4 monomethylation at derepressed Alus, making them resemble poised enhancers. The enhancer nature of e1a-targeted Alus was confirmed by the enrichment, in their upstream regions, of the EP300/CBP acetyltransferase, EP400 chromatin remodeler and YAP1 and FOS transcription factors. The physical interaction of e1a with EP400 was critical for Alu derepression, which was abrogated upon EP400 ablation. Our data suggest that e1a targets a subset of enhancer Alus whose transcriptional activation, which requires EP400 and is mediated by the e1a-EP400 interaction, may participate in the manipulation of enhancer activity by adenoviruses.
dc.language.isoENen_US
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subject.enHumans
dc.subject.enEnhancer Elements
dc.subject.enGenetic
dc.subject.enAlu Elements
dc.subject.enTranscription Factors
dc.subject.enAdenovirus E1A Proteins
dc.subject.enDNA-Binding Proteins
dc.subject.enDNA Helicases
dc.subject.enTranscription Factor AP-1
dc.subject.enChromatin Assembly and Disassembly
dc.subject.enYAP-Signaling Proteins
dc.subject.enAdaptor Proteins
dc.subject.enSignal Transducing
dc.subject.enCell Cycle Proteins
dc.subject.enTranscriptional Activation
dc.subject.enPhosphoproteins
dc.subject.enCells
dc.subject.enCultured
dc.subject.enFibroblasts
dc.subject.enHistones
dc.subject.enNuclear Proteins
dc.subject.enTranscription Factors
dc.subject.enTFIII
dc.title.enAdenovirus small E1A directs activation of Alu transcription at YAP/TEAD- and AP-1-bound enhancers through interactions with the EP400 chromatin remodeler.
dc.title.alternativeNucleic Acids Resen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1093/nar/gkae615en_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologieen_US
dc.identifier.pubmed39011896en_US
bordeaux.journalNucleic Acids Researchen_US
bordeaux.page9481-9500en_US
bordeaux.volume52en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.issue16en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcepubmed
hal.identifierhal-04714239
hal.version1
hal.date.transferred2024-09-30T09:22:23Z
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=Nucleic%20Acids%20Research&rft.date=2024-09-09&rft.volume=52&rft.issue=16&rft.spage=9481-9500&rft.epage=9481-9500&rft.eissn=1362-4962&rft.issn=1362-4962&rft.au=CANTARELLA,%20Simona&VEZZOLI,%20Marco&CARNEVALI,%20Davide&MORSELLI,%20Marco&ZEMKE,%20Nathan%20R&rft.genre=article


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