dc.contributor.author | Prendergast, Lisa | |
dc.contributor.author | Müller, Sebastian | |
dc.contributor.author | Liu, Yiwei | |
dc.contributor.author | Huang, Hongda | |
dc.contributor.author | Dingli, Florent | |
dc.contributor.author | Loew, Damarys | |
dc.contributor.author | Vassias, Isabelle | |
dc.contributor.author | Patel, Dinshaw J. | |
dc.contributor.author | Sullivan, Kevin F. | |
dc.contributor.author | Almouzni, Geneviève | |
dc.date.accessioned | 2018-09-20T16:21:55Z | |
dc.date.available | 2018-09-20T16:21:55Z | |
dc.date.issued | 2016-06-01 | |
dc.identifier.citation | Prendergast, Lisa; Müller, Sebastian; Liu, Yiwei; Huang, Hongda; Dingli, Florent; Loew, Damarys; Vassias, Isabelle; Patel, Dinshaw J. Sullivan, Kevin F.; Almouzni, Geneviève (2016). The cenp-t/-w complex is a binding partner of the histone chaperone fact. Genes & Development 30 (11), 1313-1326 | |
dc.identifier.issn | 0890-9369,1549-5477 | |
dc.identifier.uri | http://hdl.handle.net/10379/13520 | |
dc.description.abstract | The CENP-T/-W histone fold complex, as an integral part of the inner kinetochore, is essential for building a proper kinetochore at the centromere in order to direct chromosome segregation during mitosis. Notably, CENP-T/-W is not inherited at centromeres, and new deposition is absolutely required at each cell cycle for kinetochore function. However, the mechanisms underlying this new deposition of CENP-T/-W at centromeres are unclear. Here, we found that CENP-T deposition at centromeres is uncoupled from DNA synthesis. We identified Spt16 and SSRP1, subunits of the H2A-H2B histone chaperone facilitates chromatin transcription (FACT), as CENP-W binding partners through a proteomic screen. We found that the C-terminal region of Spt16 binds specifically to the histone fold region of CENP-T/-W. Furthermore, depletion of Spt16 impairs CENP-T and CENP-W deposition at endogenous centromeres, and site-directed targeting of Spt16 alone is sufficient to ensure local de novo CENP-T accumulation. We propose a model in which the FACT chaperone stabilizes the soluble CENP-T/-W complex in the cell and promotes dynamics of exchange, enabling CENP-T/-W deposition at centromeres. | |
dc.publisher | Cold Spring Harbor Laboratory | |
dc.relation.ispartof | Genes & Development | |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 Ireland | |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/3.0/ie/ | |
dc.subject | centromere | |
dc.subject | cenp | |
dc.subject | histone chaperone | |
dc.subject | mitosis | |
dc.subject | human-cells | |
dc.subject | centromeric chromatin | |
dc.subject | a nucleosomes | |
dc.subject | saccharomyces-cerevisiae | |
dc.subject | outer kinetochore | |
dc.subject | structural basis | |
dc.subject | transcription | |
dc.subject | recruitment | |
dc.subject | rna | |
dc.subject | maintenance | |
dc.title | The cenp-t/-w complex is a binding partner of the histone chaperone fact | |
dc.type | Article | |
dc.identifier.doi | 10.1101/gad.275073.115 | |
dc.local.publishedsource | http://genesdev.cshlp.org/content/30/11/1313.full.pdf | |
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