| Literature DB >> 27666591 |
Qianhua Dong1, Feng-Xiang Yin2, Feng Gao3, Yuan Shen1, Faben Zhang2, Yang Li3, Haijin He1, Marlyn Gonzalez1, Jinpu Yang1, Shu Zhang1, Min Su3, Yu-Hang Chen3, Fei Li1.
Abstract
CENP-A is a centromere-specific histone 3 variant essential for centromere specification. CENP-A partially replaces canonical histone H3 at the centromeres. How the particular CENP-A/H3 ratio at centromeres is precisely maintained is unknown. It also remains unclear how CENP-A is excluded from non-centromeric chromatin. Here, we identify Ccp1, an uncharacterized NAP family protein in fission yeast that antagonizes CENP-A loading at both centromeric and non-centromeric regions. Like the CENP-A loading factor HJURP, Ccp1 interacts with CENP-A and is recruited to centromeres at the end of mitosis in a Mis16-dependent manner. These data indicate that factors with opposing CENP-A loading activities are recruited to centromeres. Furthermore, Ccp1 also cooperates with H2A.Z to evict CENP-A assembled in euchromatin. Structural analyses indicate that Ccp1 forms a homodimer that is required for its anti-CENP-A loading activity. Our study establishes mechanisms for maintenance of CENP-A homeostasis at centromeres and the prevention of ectopic assembly of centromeres.Entities:
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Year: 2016 PMID： 27666591 PMCID： PMC5055466 DOI： 10.1016/j.molcel.2016.08.022
Source DB: PubMed Journal: Mol Cell ISSN： 1097-2765 Impact factor: 17.970