期刊
GENES & DEVELOPMENT
卷 25, 期 9, 页码 901-906出版社
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.2045111
关键词
centromere; CENP-A; histone chaperone; HJURP; structure
资金
- National Basic Research Program of China [2009CB825501, 2010CB944903, 2011CB966300, 2011CB966302, 2010CB912103]
- Natural Science Foundation of China [90919029, 3098801, 91019007]
- Chinese Academy of Sciences (CAS)
- Novo Nordisk-CAS foundation
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 beta-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.
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