Ccp1 homodimer mediates chromatin integrity by antagonizing CENP-A loading
| Autor: | Min Su, Fei Li, Yuan Shen, Marlyn Gonzalez, Haijin He, Faben Zhang, Yu-hang Chen, Feng Gao, Jinpu Yang, Yang Li, Qianhua Dong, Feng Xiang Yin, Shu Zhang |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Protein Conformation alpha-Helical Loading factor Euchromatin Chromosomal Proteins Non-Histone Centromere Mitosis macromolecular substances Carboxypeptidases Article Histones 03 medical and health sciences Histone H3 Gene Expression Regulation Fungal Schizosaccharomyces Protein Interaction Domains and Motifs Molecular Biology Genetics Binding Sites biology Cell Biology Chromatin Assembly and Disassembly Chromatin Cell biology 030104 developmental biology Histone biology.protein Protein Conformation beta-Strand Schizosaccharomyces pombe Proteins Protein Multimerization Carrier Proteins Protein Binding Signal Transduction |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|