Biochemical and structural properties of heterochromatin protein 1: understanding its role in chromatin assembly

J Biochem. 2014 Jul;156(1):11-20. doi: 10.1093/jb/mvu032. Epub 2014 May 13.

Abstract

Heterochromatin protein 1 (HP1) is an evolutionarily conserved chromosomal protein that binds lysine 9-methylated histone H3 (H3K9me), a hallmark of heterochromatin, and plays a crucial role in forming higher-order chromatin structures. HP1 has an N-terminal chromodomain and a C-terminal chromo shadow domain, linked by an unstructured hinge region. Although biochemical and structural studies have revealed each domain's properties, little is known about the mechanisms by which these domains cooperate to carry out HP1's function in forming higher-order chromatin structures. In this review, we summarize HP1's biochemical and structural properties and highlight the latest findings regarding HP1's interactions with nucleosomes.

Keywords: HP1; chromo shadow domain; chromodomain; heterochromatin; phosphorylation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Chromatin / chemistry
  • Chromatin / metabolism*
  • Chromatin Assembly and Disassembly
  • Chromosomal Proteins, Non-Histone / chemistry*
  • Chromosomal Proteins, Non-Histone / metabolism*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data

Substances

  • Chromatin
  • Chromosomal Proteins, Non-Histone
  • heterochromatin-specific nonhistone chromosomal protein HP-1