Histone deacetylases: silencers for hire

Trends Biochem Sci. 2000 Mar;25(3):121-6. doi: 10.1016/s0968-0004(00)01551-6.

Abstract

Over the past few years, the long-standing idea that covalent modification of chromatin can play a role in determining states of gene activity has been confirmed. Eukaryotic genes can be silenced by deacetylation of acetyl-lysine moieties in the N-terminal tails of histones. Recent work links histone deacetylases with an increasing number of repressors, suggesting that deacetylation might be a rather pervasive feature of transcriptional repression systems.

Publication types

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

MeSH terms

  • Animals
  • Carrier Proteins / metabolism
  • DNA-Binding Proteins / metabolism
  • Gene Silencing*
  • Histone Deacetylases / physiology*
  • Humans
  • Ikaros Transcription Factor
  • Nuclear Proteins / metabolism
  • Nuclear Receptor Co-Repressor 1
  • Proto-Oncogene Proteins / metabolism
  • Repressor Proteins / metabolism
  • Saccharomyces cerevisiae Proteins*
  • Smad3 Protein
  • Trans-Activators / metabolism
  • Transcription Factors / metabolism
  • Tumor Suppressor Protein p53 / metabolism

Substances

  • Carrier Proteins
  • DNA-Binding Proteins
  • IKZF1 protein, human
  • IKZF3 protein, human
  • NCOR1 protein, human
  • Nuclear Proteins
  • Nuclear Receptor Co-Repressor 1
  • Proto-Oncogene Proteins
  • Repressor Proteins
  • SIN3 protein, S cerevisiae
  • SMAD3 protein, human
  • Saccharomyces cerevisiae Proteins
  • Smad3 Protein
  • Trans-Activators
  • Transcription Factors
  • Tumor Suppressor Protein p53
  • SKI protein, human
  • Ikaros Transcription Factor
  • MTA2 protein, human
  • Histone Deacetylases