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How two become one: HJURP dimerization drives CENP-A assembly

dc.contributor.authorBodor, Dani L
dc.contributor.authorJansen, Lars E T
dc.date.accessioned2016-05-24T12:22:08Z
dc.date.available2016-05-24T12:22:08Z
dc.date.issued2013-06-21
dc.description.abstractCENP‐A containing nucleosomes epigenetically specify centromere position on chromosomes. Deposition of CENP‐A into chromatin is mediated by HJURP, a specific CENP‐A chaperone. Paradoxically, HJURP binding sterically prevents dimerization of CENP‐A, which is critical to form functional centromeric nucleosomes. A recent publication in The EMBO Journal (Zasadzińska et al, 2013) demonstrates that HJURP itself dimerizes through a C‐terminal repeat region, which is essential for centromeric assembly of nascent CENP‐A.pt_PT
dc.description.sponsorshipFCT fellowship: (SFRH/BD/74284/2010); FCT grants: (BIA-BCM/100557/2008, BIAPRO/100537/2008); EMBO Installation Grant.pt_PT
dc.identifier.citationBodor, D. L., Jansen, L. E. T. (2013). How two become one: HJURP dimerization drives CENP-A assembly. EMBO J., 32(15), 2090–2092.pt_PT
dc.identifier.doi10.1038/emboj.2013.150pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.7/618
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherEmbo Presspt_PT
dc.relation.publisherversionhttp://emboj.embopress.org/content/32/15/2090pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectAutoantigenspt_PT
dc.subjectCentromerept_PT
dc.subjectChromosomal Proteins, Non-Histonept_PT
dc.subjectDNA-Binding Proteinspt_PT
dc.subjectHumanspt_PT
dc.subjectNucleosomespt_PT
dc.subjectProtein Multimerizationpt_PT
dc.titleHow two become one: HJURP dimerization drives CENP-A assemblypt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage2092pt_PT
oaire.citation.issue15pt_PT
oaire.citation.startPage2090pt_PT
oaire.citation.titleThe EMBO Journalpt_PT
oaire.citation.volume32pt_PT
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT

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