Functional consequences of histone modifications

Curr Opin Genet Dev. 2003 Apr;13(2):154-60. doi: 10.1016/s0959-437x(03)00020-0.

Abstract

Covalent modifications of the histone proteins have well-known roles in gene expression. Experiments reported during the past year have extended this paradigm to include roles for histone acetylation and phosphorylation in DNA double-strand break repair. In addition, new results now provide a definitive example of an acetylation histone code, whereas others reveal the workings of a charge patch mechanism. Finally, exciting research has identified new modifications, complex modification cascades, and functional links to DNA methylation and RNA interference pathways.

Publication types

  • Review

MeSH terms

  • Acetylation
  • Acetyltransferases / physiology
  • Animals
  • Histones / physiology*
  • Humans
  • Methylation
  • Methyltransferases / physiology
  • Phosphorylation
  • Phosphotransferases / physiology
  • RNA / physiology
  • Schizosaccharomyces / physiology

Substances

  • Histones
  • RNA
  • Methyltransferases
  • Acetyltransferases
  • Phosphotransferases