Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP.
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.
Mesh Terms:
Autoantigens, Chromosomal Proteins, Non-Histone, DNA, DNA-Binding Proteins, Histones, Humans, Models, Molecular, Protein Binding, Protein Structure, Quaternary
Autoantigens, Chromosomal Proteins, Non-Histone, DNA, DNA-Binding Proteins, Histones, Humans, Models, Molecular, Protein Binding, Protein Structure, Quaternary
Genes Dev.
Date: May. 01, 2011
PubMed ID: 21478274
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