Dynamics of histone acetylation in vivo. A function for acetylation turnover?

Biochem Cell Biol. 2002;80(3):363-78. doi: 10.1139/o02-080.


Histone acetylation, discovered more than 40 years ago, is a reversible modification of lysines within the amino-terminal domain of core histones. Amino-terminal histone domains contribute to the compaction of genes into repressed chromatin fibers. It is thought that their acetylation causes localized relaxation of chromatin as a necessary but not sufficient condition for processes that repackage DNA such as transcription, replication, repair, recombination, and sperm formation. While increased histone acetylation enhances gene transcription and loss of acetylation represses and silences genes, the function of the rapid continuous or repetitive acetylation and deacetylation reactions with half-lives of just a few minutes remains unknown. Thirty years of in vivo measurements of acetylation turnover and rates of change in histone modification levels have been reviewed to identify common chromatin characteristics measured by distinct protocols. It has now become possible to look across a wider spectrum of organisms than ever before and identify common features. The rapid turnover rates in transcriptionally active and competent chromatin are one such feature. While ubiquitously observed, we still do not know whether turnover itself is linked to chromatin transcription beyond its contribution to rapid changes towards hyper- or hypoacetylation of nucleosomes. However, recent experiments suggest that turnover may be linked directly to steps in gene transcription, interacting with nucleosome remodeling complexes.

Publication types

  • Review

MeSH terms

  • Acetylation
  • Acetyltransferases / metabolism*
  • Animals
  • Histone Deacetylase Inhibitors
  • Histones / chemistry*
  • Humans
  • Kinetics
  • Medicago sativa
  • Phosphorus Radioisotopes / metabolism
  • RNA, Messenger / metabolism
  • Staining and Labeling
  • Tetrahymena
  • Transcription, Genetic / physiology


  • Histone Deacetylase Inhibitors
  • Histones
  • Phosphorus Radioisotopes
  • RNA, Messenger
  • Acetyltransferases