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Human H4 tail stimulates HIV-1 integration through binding to the carboxy-terminal domain of integrase.

dc.rights.licenseopenen_US
dc.contributor.authorMAURO, Eric
dc.contributor.authorLESBATS, Paul
dc.contributor.authorLAPAILLERIE, Delphine
dc.contributor.authorCHAIGNEPAIN, Stephane
dc.contributor.authorMAILLOT, Benoit
dc.contributor.authorOLADOSU, Oyindamola
dc.contributor.authorROBERT, Xavier
dc.contributor.authorFIORIN, Francesca
dc.contributor.authorKIEFFER, Bruno
dc.contributor.authorBOUAZIZ, Serge
dc.contributor.authorGOUET, Patrice
dc.contributor.authorRUFF, Marc
dc.contributor.authorPARISSI, Vincent
dc.date.accessioned2019
dc.date.available2019
dc.date.issued2019
dc.identifier.otherhttps://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/nar/47/7/10.1093_nar_gkz091/1/gkz091_supplemental_file.pdf?Expires=1586791363&Signature=2RwZT4ihov0zCox8Zr~3zfFJai5XIAD~ONeZvfc51l6cyrk0CtRD3qW1Uh-u-rmfj2EYok80S7KFnqz5ZtYD1vGhuUfr5RPyN~GfAZnj3ahEBRi7oqNYxng6~IesaRXt28nDqhiwp~aevqDM68121s1uVyA2LRQxdZI5i6B6RMfBsS5oM96yof3nL3ayCRj5a8ZargIZQiguyoEzg02NSxAL2srBBtVkWzu9XpN6XlyNiRYBwCTtLWmSp3YGOc3vJdzIxQTGkVbh7McVPDBgyl1FmDeil94E1FrLCAf3wsXc2HOmiD4SL3ZHrm6iXws1y3kqPwPehp1KMmt89ngM6Q__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGAen_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/3804
dc.description.abstractEnThe integration of the retroviral genome into the chro-matin of the infected cell is catalysed by the inte-grase (IN)•viral DNA complex (intasome). This pro-cess requires functional association between theintegration complex and the nucleosomes. Directintasome/histone contacts have been reported tomodulate the interaction between the integrationcomplex and the target DNA (tDNA). Both prototypefoamy virus (PFV) and HIV-1 integrases can directlybind histone amino-terminal tails. We have furtherinvestigated this final association by studying the ef-fect of isolated histone tails on HIV-1 integration. Weshow here that the binding of HIV-1 IN to a peptidederived from the H4 tail strongly stimulates integra-tion catalysisin vitro. This stimulation was not ob-served with peptide tails from other variants or withalpha-retroviral (RAV) and spuma-retroviral PFV in-tegrases. Biochemical analyses show that the pep-tide tail induces both an increase in the IN oligomer-ization state and affinity for the target DNA, whichare associated with substantial structural rearrange-ments in the IN carboxy-terminal domain (CTD) ob-served by NMR. Our data indicate that the H4 peptidetail promotes the formation of active strand transfercomplexes (STCs) and support an activation step ofthe incoming intasome at the contact of the histonetail.
dc.description.sponsorshipInfrastructure Française pour la Biologie Structurale Intégrée - ANR-10-INBS-05-01/10-INBS-0005en_US
dc.language.isoENen_US
dc.rightsAttribution-NonCommercial 3.0 United States
dc.rights.urihttp://creativecommons.org/licenses/by-nc/3.0/us/
dc.subjectBobinage
dc.subjectMatériaux Composites
dc.subjectRéservoir
dc.title.enHuman H4 tail stimulates HIV-1 integration through binding to the carboxy-terminal domain of integrase.
dc.typeArticle de revueen_US
dc.identifier.doi10.1093/nar/gkz091
dc.subject.halSciences de l'ingénieur [physics]/Matériauxen_US
dc.subject.halSciences de l'ingénieur [physics]/Mécanique [physics.med-ph]/Mécanique des fluides [physics.class-ph]en_US
dc.subject.halSciences de l'ingénieur [physics]/Mécanique [physics.med-ph]/Mécanique des matériaux [physics.class-ph]en_US
bordeaux.journalNucleic Acids Researchen_US
bordeaux.page3607-3618en_US
bordeaux.volume47en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248
bordeaux.issue7en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionCNRS
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03181418
hal.version1
hal.date.transferred2021-03-29T12:54:51Z
hal.exporttrue
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