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

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 ?-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.

SUBMITTER: Hu H

PROVIDER: S-EPMC3084024 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature

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

Hu Hao H Liu Yang Y Wang Mingzhu M Fang Junnan J Huang Hongda H Yang Na N Li Yanbo Y Wang Jianyu J Yao Xuebiao X Shi Yunyu Y Li Guohong G Xu Rui-Ming RM

Genes & development 20110408 9

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 analy ...[more]

PMID: 21478274

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