For a healthy histone code, a little SUMO in the tail keeps the acetyl away

ACS Chem Biol. 2006 May 23;1(4):204-6. doi: 10.1021/cb600188m.

Abstract

Chemical modification of histones through a growing number of post-translational mechanisms is an integral part of transcription. A recent report provides exciting new evidence that conjugation of the ubiquitin-like protein SUMO to histones opposes acetylation and establishes SUMOylation as an important histone mark linked to transcriptional repression.

Publication types

  • Review

MeSH terms

  • Acetylation
  • Animals
  • Histone Code / physiology*
  • Humans
  • Small Ubiquitin-Related Modifier Proteins / chemistry*
  • Small Ubiquitin-Related Modifier Proteins / genetics
  • Small Ubiquitin-Related Modifier Proteins / metabolism*

Substances

  • Small Ubiquitin-Related Modifier Proteins