5GPL

Crystal structure of Ccp1

Summary for 5GPL

• Entry DOI: 10.2210/pdb5gpl/pdb
• Related: 5GPK
• Descriptor: Putative nucleosome assembly protein C36B7.08c (2 entities in total)
• Functional Keywords: ccp1 dimer, nucleosome assembly protein, chaperone
• Biological source: Schizosaccharomyces pombe 972h- (Fission yeast)
• Cellular location: Nucleus : Q9HGN2
• Total number of polymer chains: 2
• Total formula weight: 64710.50

Authors

Yin, F.,Gao, F.,Chen, Y. (deposition date: 2016-08-03, release date: 2016-11-30, Last modification date: 2023-11-08)

Primary citation

Dong, Q.,Yin, F.X.,Gao, F.,Shen, Y.,Zhang, F.,Li, Y.,He, H.,Gonzalez, M.,Yang, J.,Zhang, S.,Su, M.,Chen, Y.H.,Li, F.
Ccp1 Homodimer Mediates Chromatin Integrity by Antagonizing CENP-A Loading
Mol.Cell, 64:79-91, 2016

PubMed 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.

PubMed: 27666591
DOI: 10.1016/j.molcel.2016.08.022

Experimental method

X-RAY DIFFRACTION (2.1 Å)