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Authordc.contributor.authorBenleulmi, Mohamed S. 
Authordc.contributor.authorMatysiak, Julien 
Authordc.contributor.authorRobert, Xavier 
Authordc.contributor.authorMiskey, Csaba 
Authordc.contributor.authorMauro, Eric 
Authordc.contributor.authorLapaillerie, Delphine 
Authordc.contributor.authorLesbats, Paul 
Authordc.contributor.authorChaignepain, Stephane 
Authordc.contributor.authorHenríquez, Daniel R. 
Authordc.contributor.authorCalmels, Christina 
Authordc.contributor.authorOladosu, Oyindamola 
Authordc.contributor.authorThierry, Eloise 
Authordc.contributor.authorLeon Decap, Oscar 
Authordc.contributor.authorLavigne, Marc 
Authordc.contributor.authorAndreola, Marie Line 
Authordc.contributor.authorDelelis, Olivier 
Authordc.contributor.authorIvics, Zoltan 
Authordc.contributor.authorRuff, Marc 
Authordc.contributor.authorGouet, Patrice 
Authordc.contributor.authorParissi, Vincent 
Cita de ítemdc.identifier.citationRetrovirology (2017) 14:54es_ES
Abstractdc.description.abstractBackground: Stable insertion of the retroviral DNA genome into host chromatin requires the functional association between the intasome (integrase viral DNA complex) and the nucleosome. The data from the literature suggest that direct protein protein contacts between integrase and histones may be involved in anchoring the intasome to the nucleosome. Since histone tails are candidates for interactions with the incoming intasomes we have investigated whether they could participate in modulating the nucleosomal integration process. Results: We show here that histone tails are required for an optimal association between HIV-1 integrase (IN) and the nucleosome for efficient integration. We also demonstrate direct interactions between IN and the amino-terminal tail of human histone H4 in vitro. Structure/function studies enabled us to identify amino acids in the carboxy-terminal domain of IN that are important for this interaction. Analysis of the nucleosome-binding properties of catalytically active mutated INs confirmed that their ability to engage the nucleosome for integration in vitro was affected. Pseudovirus particles bearing mutations that affect the IN/H4 association also showed impaired replication capacity due to altered integration and re-targeting of their insertion sites toward dynamic regions of the chromatin with lower nucleosome occupancy. Conclusions: Collectively, our data support a functional association between HIV-1 IN and histone tails that promotes anchoring of the intasome to nucleosomes and optimal integration into chromatin.es_ES
Patrocinadordc.description.sponsorshipFrench National Research Agency [ANR, RETROSelect program] French National Research Agency against AIDS (ANRS) AO 2016-2 ECTZ18624 SIDACTION AO-27-1 10465 16-1-AEQ-10465 French Infrastructure for Integrated Structural Biology (FRISBI) ANR-10-INSB-05-01 Instruct, European Strategy Forum on Research Infrastructures (ESFRI) Centre National de la Recherche Scientifique (CNRS) University Victor Segalen Bordeaux 2 ECOS-CONICYT C12B03 programes_ES
Publisherdc.publisherBiomed Central Ltd.es_ES
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile*
Link to Licensedc.rights.uri*
Keywordsdc.subjectRetroviral integrationes_ES
Keywordsdc.subjectHistone tailses_ES
Títulodc.titleModulation of the functional association between the HIV-1 intasome and the nucleosome by histone amino-terminal tailses_ES
Document typedc.typeArtículo de revista
Indexationuchile.indexArtículo de publicación ISIes_ES

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Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile