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

  • Genes Dev. 2011 May 1;25(9):901-6. doi: 10.1101/gad.2045111.
Hao Hu  1 ,  Yang Liu ,  Mingzhu Wang ,  Junnan Fang ,  Hongda Huang ,  Na Yang ,  Yanbo Li ,  Jianyu Wang ,  Xuebiao Yao ,  Yunyu Shi ,  Guohong Li ,  Rui-Ming Xu
Affiliations
  • 1. National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
PMID: 21478274 DOI: 10.1101/gad.2045111
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.