Histone acetyltransferase complexes: one size doesn't fit all

Nat Rev Mol Cell Biol. 2007 Apr;8(4):284-95. doi: 10.1038/nrm2145.


Over the past 10 years, the study of histone acetyltransferases (HATs) has advanced significantly, and a number of HATs have been isolated from various organisms. It emerged that HATs are highly diverse and generally contain multiple subunits. The functions of the catalytic subunit depend largely on the context of the other subunits in the complex. We are just beginning to understand the specialized roles of HAT complexes in chromosome decondensation, DNA-damage repair and the modification of non-histone substrates, as well as their role in the broader epigenetic landscape, including the role of protein domains within HAT complexes and the dynamic interplay between HAT complexes and existing histone modifications.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Chromatin / metabolism*
  • DNA Repair*
  • Histone Acetyltransferases / chemistry
  • Histone Acetyltransferases / metabolism*
  • Histones / metabolism*
  • Humans
  • Models, Molecular
  • Protein Structure, Tertiary
  • Substrate Specificity


  • Chromatin
  • Histones
  • Histone Acetyltransferases