Erasers of histone acetylation: the histone deacetylase enzymes

Cold Spring Harb Perspect Biol. 2014 Apr 1;6(4):a018713. doi: 10.1101/cshperspect.a018713.

Abstract

Histone deacetylases (HDACs) are enzymes that catalyze the removal of acetyl functional groups from the lysine residues of both histone and nonhistone proteins. In humans, there are 18 HDAC enzymes that use either zinc- or NAD(+)-dependent mechanisms to deacetylate acetyl lysine substrates. Although removal of histone acetyl epigenetic modification by HDACs regulates chromatin structure and transcription, deacetylation of nonhistones controls diverse cellular processes. HDAC inhibitors are already known potential anticancer agents and show promise for the treatment of many diseases.

Publication types

  • Review

MeSH terms

  • Arginase / chemistry
  • Arginase / classification
  • Arginase / physiology
  • Gene Expression Regulation
  • Histone Deacetylase Inhibitors / chemistry
  • Histone Deacetylase Inhibitors / metabolism
  • Histone Deacetylases / chemistry
  • Histone Deacetylases / classification
  • Histone Deacetylases / physiology*
  • Histones / chemistry
  • Histones / metabolism
  • Humans
  • Models, Biological
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae / enzymology
  • Sirtuins / antagonists & inhibitors
  • Sirtuins / chemistry
  • Substrate Specificity

Substances

  • Histone Deacetylase Inhibitors
  • Histones
  • Sirtuins
  • Histone Deacetylases
  • Arginase