Structure and function of histone acetyltransferases

Cell Mol Life Sci. 2001 May;58(5-6):693-703. doi: 10.1007/pl00000893.

Abstract

Histone acetyltranferase (HAT) enzymes are the catalytic subunit of large multisubunit HAT complexes that acetylate the epsilon-amino group of specific lysine residues on histone tails to promote transcriptional activation. Recent structural and functional studies on the divergent HAT enzymes Gcn5/PCAF, Esa1 and Hat1 have provided new insights into the underlying mechanism of histone binding and acetylation by HAT proteins. The three HAT enzymes contain a structurally conserved core domain that plays a functionally conserved role in binding the coenzyme A cofactor and in harboring the putative general base for catalysis. Structurally variable N- and C-terminal domains appear to contain a related scaffold that mediates histone substrate binding. These data provide a framework for understanding the structure and function of other more divergent HAT proteins such as TAF(II)250 and CBP/p300, and provides a starting point for understanding how HAT proteins may cooperate with other factors within in vivo HAT complexes to promote transcriptional activation.

Publication types

  • Review

MeSH terms

  • Acetyltransferases / chemistry*
  • Acetyltransferases / genetics
  • Acetyltransferases / metabolism*
  • Animals
  • Binding Sites
  • Catalysis
  • Coenzyme A / metabolism
  • Histone Acetyltransferases
  • Histones / chemistry
  • Histones / metabolism
  • Humans
  • Models, Molecular
  • Multigene Family
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae Proteins*
  • Structure-Activity Relationship
  • Substrate Specificity
  • Transcription, Genetic

Substances

  • Histones
  • Saccharomyces cerevisiae Proteins
  • Acetyltransferases
  • Histone Acetyltransferases
  • Coenzyme A