Structural highlights
FunctionPublication Abstract from PubMedCENP-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. Ccp1 Homodimer Mediates Chromatin Integrity by Antagonizing CENP-A Loading.,Dong Q, Yin FX, Gao F, Shen Y, Zhang F, Li Y, He H, Gonzalez M, Yang J, Zhang S, Su M, Chen YH, Li F Mol Cell. 2016 Oct 6;64(1):79-91. doi: 10.1016/j.molcel.2016.08.022. Epub 2016, Sep 22. PMID:27666591[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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