Ccp1 Homodimer Mediates Chromatin Integrity by Antagonizing CENP-A Loading

Qianhua Dong; Feng Xiang Yin; Feng Gao; Yuan Shen; Faben Zhang; Yang Li; Haijin He; Marlyn Gonzalez; Jinpu Yang; Shu Zhang; Min Su; Yu Hang Chen; Fei Li

doi:10.1016/j.molcel.2016.08.022

Ccp1 Homodimer Mediates Chromatin Integrity by Antagonizing CENP-A Loading

Qianhua Dong, Feng Xiang Yin, Feng Gao, Yuan Shen, Faben Zhang, Yang Li, Haijin He, Marlyn Gonzalez, Jinpu Yang, Shu Zhang, Min Su, Yu Hang Chen, Fei Li

Biology and Genomics

Research output: Contribution to journal › Article › peer-review

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.

Original language	English (US)
Pages (from-to)	79-91
Number of pages	13
Journal	Molecular Cell
Volume	64
Issue number	1
DOIs	https://doi.org/10.1016/j.molcel.2016.08.022
State	Published - Oct 6 2016

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/j.molcel.2016.08.022

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title = "Ccp1 Homodimer Mediates Chromatin Integrity by Antagonizing CENP-A Loading",

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.",

author = "Qianhua Dong and Yin, {Feng Xiang} and Feng Gao and Yuan Shen and Faben Zhang and Yang Li and Haijin He and Marlyn Gonzalez and Jinpu Yang and Shu Zhang and Min Su and Chen, {Yu Hang} and Fei Li",

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AU - Dong, Qianhua

AU - Yin, Feng Xiang

AU - Gao, Feng

AU - Shen, Yuan

AU - Zhang, Faben

AU - Li, Yang

AU - He, Haijin

AU - Gonzalez, Marlyn

AU - Yang, Jinpu

AU - Zhang, Shu

AU - Su, Min

AU - Chen, Yu Hang

AU - Li, Fei

PY - 2016/10/6

Y1 - 2016/10/6

N2 - 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.

AB - 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.

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Ccp1 Homodimer Mediates Chromatin Integrity by Antagonizing CENP-A Loading

Abstract

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