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Structure of a CENP-A -- histone H4 heterodimer in complex with chaperone HJURP.

Authors :
Hao Hu
Yang Liu
Mingzhu Wang
Junnan Fang
Hongda Huang
Na Yang
Yanbo Li
Jianyu Wang
Xuebiao Yao
Yunyu Shi
Guohong Li
Rui-Ming Xu
Source :
Genes & Development. 5/1/2011, Vol. 25 Issue 9, p4-4. 1p.
Publication Year :
2011

Abstract

In higher eukaryotes, the centromere is epigenetically specified by the histone H3 variant Centromere Protein-A (CENP-A). Deposition of CENP-A to the centromere requires histone chaperone HJURP (Holliday junction recognition protein). The crystal structure of an HJURP-CENP-A-histone H4 complex shows that HJURP binds a CENP-A-H4 heterodimer. The C-terminal β-sheet domain of HJURP caps the DNA-binding region of the histone heterodimer, preventing it from spontaneous association with DNA. Our analysis also revealed a novel site in CENP-A that distinguishes it from histone H3 in its ability to bind HJURP. These findings provide key information for specific recognition of CENP-A and mechanistic insights into the process of centromeric chromatin assembly. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
08909369
Volume :
25
Issue :
9
Database :
Academic Search Index
Journal :
Genes & Development
Publication Type :
Academic Journal
Accession number :
60995493
Full Text :
https://doi.org/10.1101/gad.2045111