The emerging role of class II histone deacetylases

Biochem Cell Biol. 2001;79(3):337-48.

Abstract

Histone acetylation and deacetylation play essential roles in modifying chromatin structure and regulating gene expression in all eukaryotes. Several histone acetyltransferases have been identified that act as transcriptional coactivators. In contrast, histone deacetylases (HDACs) are part of transcriptional corepressor complexes. Based on their similarity to known yeast factors, the human HDACs are grouped into three classes. Class I HDACs are similar to the yeast transcriptional repressor yRPD3, while class II HDACs are related to yHDA1 and class III HDACs to ySIR2. In this review, we focus on the biology of class II HDACs. These newly discovered enzymes have been implicated in cell differentiation and development, and many molecular details are emerging that shed light on class II HDAC function and regulation. We discuss the biological role of these factors in the context of physiological processes.

Publication types

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

MeSH terms

  • 14-3-3 Proteins
  • Alcohol Oxidoreductases
  • Apoptosis / genetics
  • Calmodulin / metabolism
  • DNA-Binding Proteins / metabolism
  • Histone Deacetylases / classification
  • Histone Deacetylases / genetics*
  • Histone Deacetylases / metabolism*
  • Humans
  • MEF2 Transcription Factors
  • Muscle Development / genetics
  • Myogenic Regulatory Factors
  • Phosphoproteins / metabolism
  • Protein Structure, Tertiary
  • Repressor Proteins / metabolism
  • Tissue Distribution
  • Transcription Factors / metabolism
  • Transcription, Genetic / genetics
  • Tyrosine 3-Monooxygenase / metabolism

Substances

  • 14-3-3 Proteins
  • Calmodulin
  • DNA-Binding Proteins
  • MEF2 Transcription Factors
  • Myogenic Regulatory Factors
  • Phosphoproteins
  • Repressor Proteins
  • Transcription Factors
  • Alcohol Oxidoreductases
  • C-terminal binding protein
  • Tyrosine 3-Monooxygenase
  • Histone Deacetylases