Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression

Nat Struct Mol Biol. 2014 Jun;21(6):569-71. doi: 10.1038/nsmb.2833. Epub 2014 May 18.

Abstract

A key step in gene repression by Polycomb is trimethylation of histone H3 K27 by PCR2 to form H3K27me3. H3K27me3 provides a binding surface for PRC1. We show that monoubiquitination of histone H2A by PRC1-type complexes to form H2Aub creates a binding site for Jarid2-Aebp2-containing PRC2 and promotes H3K27 trimethylation on H2Aub nucleosomes. Jarid2, Aebp2 and H2Aub thus constitute components of a positive feedback loop establishing H3K27me3 chromatin domains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Drosophila / genetics*
  • Epigenetic Repression*
  • Histones / metabolism*
  • Methylation
  • Polycomb-Group Proteins / genetics*
  • Ubiquitination

Substances

  • Histones
  • Polycomb-Group Proteins