Histone acetyltransferases: function, structure, and catalysis

Curr Opin Genet Dev. 2001 Apr;11(2):155-61. doi: 10.1016/s0959-437x(00)00173-8.

Abstract

Histone acetyltransferases (HATs) directly link chromatin modification to gene activation. Recent structure/function studies provide insights into HAT catalysis and histone binding, and genetic studies suggest cross-talk between acetylation and other histone modifications. Developmental aberrations in mice and certain human cancers are associated with HAT mutations, further highlighting the importance of these enzymes to normal cell growth and differentiation.

Publication types

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

MeSH terms

  • Acetylation
  • Acetyltransferases / chemistry*
  • Acetyltransferases / genetics
  • Acetyltransferases / metabolism*
  • Animals
  • Catalysis
  • Chromatin / genetics
  • Chromatin / metabolism
  • Embryonic and Fetal Development
  • Histone Acetyltransferases
  • Histones / metabolism*
  • Humans
  • Mice
  • Neoplasms / etiology
  • Saccharomyces cerevisiae Proteins*
  • Transcription, Genetic
  • Yeasts / enzymology

Substances

  • Chromatin
  • Histones
  • Saccharomyces cerevisiae Proteins
  • Acetyltransferases
  • Histone Acetyltransferases