| Literature DB >> 19410545 |
Elaine M Dunleavy1, Danièle Roche, Hideaki Tagami, Nicolas Lacoste, Dominique Ray-Gallet, Yusuke Nakamura, Yataro Daigo, Yoshihiro Nakatani, Geneviève Almouzni-Pettinotti.
Abstract
The histone H3 variant CenH3, called CENP-A in humans, is central in centromeric chromatin to ensure proper chromosome segregation. In the absence of an underlying DNA sequence, it is still unclear how CENP-A deposition at centromeres is determined. Here, we purified non-nucleosomal CENP-A complexes to identify direct CENP-A partners involved in such a mechanism and identified HJURP. HJURP was not detected in H3.1- or H3.3-containing complexes, indicating its specificity for CENP-A. HJURP centromeric localization is cell cycle regulated, and its transient appearance at the centromere coincides precisely with the proposed time window for new CENP-A deposition. Furthermore, HJURP downregulation leads to a major reduction in CENP-A at centromeres and impairs deposition of newly synthesized CENP-A, causing mitotic defects. We conclude that HJURP is a key factor for CENP-A deposition and maintenance at centromeres.Entities:
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Year: 2009 PMID： 19410545 DOI： 10.1016/j.cell.2009.02.040
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582