Molecular Implementation and Physiological Roles for Histone H3 Lysine 4 (H3K4) Methylation

Curr Opin Cell Biol. 2008 Jun;20(3):341-8. doi: 10.1016/j.ceb.2008.03.019. Epub 2008 May 26.

Abstract

Chromosomal surfaces are ornamented with a variety of post-translational modifications of histones, which are required for the regulation of many of the DNA-templated processes. Such histone modifications include acetylation, sumoylation, phosphorylation, ubiquitination, and methylation. Histone modifications can either function by disrupting chromosomal contacts or by regulating non-histone protein interactions with chromatin. In this review, recent findings will be discussed regarding the regulation of the implementation and physiological significance for one such histone modification, histone H3 lysine 4 (H3K4) methylation by the yeast COMPASS and mammalian COMPASS-like complexes.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Amino Acid Sequence / genetics
  • Animals
  • Chromatin / genetics
  • Chromatin / metabolism*
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Epigenesis, Genetic / genetics*
  • Gene Expression Regulation, Fungal / genetics
  • Histone-Lysine N-Methyltransferase
  • Histones / chemistry
  • Histones / genetics
  • Histones / metabolism*
  • Humans
  • Lysine / metabolism*
  • Macromolecular Substances / metabolism
  • Methylation
  • Protein Processing, Post-Translational / genetics*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Transcription Factors / genetics
  • Transcription Factors / metabolism

Substances

  • Chromatin
  • DNA-Binding Proteins
  • Histones
  • Macromolecular Substances
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Histone-Lysine N-Methyltransferase
  • SET1 protein, S cerevisiae
  • Lysine