| Literature DB >> 21478274 |
Hao Hu1, Yang Liu, Mingzhu Wang, Junnan Fang, Hongda Huang, Na Yang, Yanbo Li, Jianyu Wang, Xuebiao Yao, Yunyu Shi, Guohong Li, Rui-Ming Xu.
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.Entities:
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Year: 2011 PMID： 21478274 PMCID： PMC3084024 DOI： 10.1101/gad.2045111
Source DB: PubMed Journal: Genes Dev ISSN： 0890-9369 Impact factor: 11.361