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. Epub 2011 Apr 8.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Autoantigens / chemistry*
  • Autoantigens / metabolism
  • Centromere Protein A
  • 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

Substances

  • Autoantigens
  • CENPA protein, human
  • Centromere Protein A
  • Chromosomal Proteins, Non-Histone
  • DNA-Binding Proteins
  • HJURP protein, human
  • Histones
  • DNA