Ring1B compacts chromatin structure and represses gene expression independent of histone ubiquitination

Mol Cell. 2010 May 14;38(3):452-64. doi: 10.1016/j.molcel.2010.02.032.

Abstract

How polycomb group proteins repress gene expression in vivo is not known. While histone-modifying activities of the polycomb repressive complexes (PRCs) have been studied extensively, in vitro data have suggested a direct activity of the PRC1 complex in compacting chromatin. Here, we investigate higher-order chromatin compaction of polycomb targets in vivo. We show that PRCs are required to maintain a compact chromatin state at Hox loci in embryonic stem cells (ESCs). There is specific decompaction in the absence of PRC2 or PRC1. This is due to a PRC1-like complex, since decompaction occurs in Ring1B null cells that still have PRC2-mediated H3K27 methylation. Moreover, we show that the ability of Ring1B to restore a compact chromatin state and to repress Hox gene expression is not dependent on its histone ubiquitination activity. We suggest that Ring1B-mediated chromatin compaction acts to directly limit transcription in vivo.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Animals
  • Cell Differentiation
  • Cell Line
  • Chromatin Assembly and Disassembly*
  • Down-Regulation
  • Embryonic Stem Cells / metabolism*
  • Histones / metabolism*
  • Homeodomain Proteins / genetics
  • Homeodomain Proteins / metabolism
  • Methylation
  • Mice
  • Mutation
  • Polycomb Repressive Complex 1
  • Polycomb Repressive Complex 2
  • Polycomb-Group Proteins
  • Protein Processing, Post-Translational*
  • Repressor Proteins / genetics
  • Repressor Proteins / metabolism*
  • Transcription, Genetic
  • Ubiquitin-Protein Ligases
  • Ubiquitination

Substances

  • Eed protein, mouse
  • Histones
  • Homeodomain Proteins
  • Polycomb-Group Proteins
  • Repressor Proteins
  • Polycomb Repressive Complex 2
  • Polycomb Repressive Complex 1
  • Rnf2 protein, mouse
  • Ubiquitin-Protein Ligases

Associated data

  • GEO/GSE20201
  • GEO/GSE20213