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Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes

2013-04-01Journal article Open access
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dc.contributor.authorBodor, D. L.
dc.contributor.authorValente, L. P.
dc.contributor.authorMata, J. F.
dc.contributor.authorBlack, B. E.
dc.contributor.authorJansen, L. E. T.
dc.date.accessioned2015-10-22T15:50:15Z
dc.date.available2015-10-22T15:50:15Z
dc.date.issued2013-04-01
dc.description.abstractCentromeres are the site of kinetochore formation during mitosis. Centromere protein A (CENP-A), the centromere-specific histone H3 variant, is essential for the epigenetic maintenance of centromere position. Previously we showed that newly synthesized CENP-A is targeted to centromeres exclusively during early G1 phase and is subsequently maintained across mitotic divisions. Using SNAP-based fluorescent pulse labeling, we now demonstrate that cell cycle-restricted chromatin assembly at centromeres is unique to CENP-A nucleosomes and does not involve assembly of other H3 variants. Strikingly, stable retention is restricted to the CENP-A/H4 core of the nucleosome, which we find to outlast general chromatin across several cell divisions. We further show that cell cycle timing of CENP-A assembly is independent of centromeric DNA sequences and instead is mediated by the CENP-A targeting domain. Unexpectedly, this domain also induces stable transmission of centromeric nucleosomes, independent of the CENP-A deposition factor HJURP. This demonstrates that intrinsic properties of the CENP-A protein direct its cell cycle-restricted assembly and induces quantitative mitotic transmission of the CENP-A/H4 nucleosome core, ensuring long-term stability and epigenetic maintenance of centromere position.pt_PT
dc.description.sponsorshipFCT fellpwships: (SFRH/BD/74284/2010, SFRH/BPD/69115/2010), National Institutes of Health grant: (GM082989), Burroughs Wellcome Fund (Career Award in the Biomedical Sciences), Rita Allen Foundation Scholar Award, Instituto Gulbenkian de Ciência, European Commission FP7 Program, EMBO.pt_PT
dc.identifier10.1091/mbc.E13-01-0034
dc.identifier.citationDani L. Bodor, Luis P. Valente, João F. Mata, Ben E. Black, and Lars E. T. Jansen Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes Mol. Biol. Cell 2013 24:7 923-932; First Published on January 30, 2013; doi:10.1091/mbc.E13-01-0034pt_PT
dc.identifier.doi10.1091/mbc.E13-01-0034
dc.identifier.urihttp://hdl.handle.net/10400.7/430
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherAmerican Society for Cell Biologypt_PT
dc.relation.publisherversionhttp://www.molbiolcell.org/content/24/7/923.longpt_PT
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/pt_PT
dc.subjectG1 Phasept_PT
dc.subjectNucleosomespt_PT
dc.titleAssembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomespt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-BCM%2F100557%2F2008/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-PRO%2F100537%2F2008/PT
oaire.citation.endPage932pt_PT
oaire.citation.issue7pt_PT
oaire.citation.startPage923pt_PT
oaire.citation.titleMolecular Biology of the Cellpt_PT
oaire.citation.volume24pt_PT
oaire.fundingStream3599-PPCDT
oaire.fundingStream3599-PPCDT
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isProjectOfPublication920402dc-3fe1-4134-b1c7-1e51333ae32f
relation.isProjectOfPublication335e7483-9cd3-449a-b37a-bea73b224517
relation.isProjectOfPublication.latestForDiscovery920402dc-3fe1-4134-b1c7-1e51333ae32f

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