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PMID:21478274

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Citation

Hu, H, Liu, Y, Wang, M, Fang, J, Huang, H, Yang, N, Li, Y, Wang, J, Yao, X, Shi, Y, Li, G and Xu, RM (2011) Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP. Genes Dev. 25:901-6

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.

Links

PubMed PMC3084024 Online version:10.1101/gad.2045111

Keywords

Autoantigens/chemistry; Autoantigens/metabolism; Chromosomal Proteins, Non-Histone/chemistry; Chromosomal Proteins, Non-Histone/metabolism; DNA/metabolism; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/metabolism; Histones/chemistry; Histones/metabolism; Humans; Models, Molecular; Protein Binding; Protein Structure, Quaternary

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