Regulation of histone methylation by demethylimination and demethylation

Nat Rev Mol Cell Biol. 2007 Apr;8(4):307-18. doi: 10.1038/nrm2143. Epub 2007 Mar 7.

Abstract

Histone methylation has important roles in regulating transcription, genome integrity and epigenetic inheritance. Historically, methylated histone arginine and lysine residues have been considered static modifications because of the low levels of methyl-group turnover in chromatin. The recent identification of enzymes that antagonize or remove histone methylation has changed this view and now the dynamic nature of these modifications is being appreciated. Here, we examine the enzymatic and structural basis for the mechanisms that these enzymes use to counteract histone methylation and provide insights into their substrate specificity and biological function.

Publication types

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

MeSH terms

  • Animals
  • Arginine / metabolism
  • Histones / metabolism*
  • Humans
  • Hydrolases / chemistry
  • Hydrolases / metabolism*
  • Lysine / metabolism
  • Methylation
  • Oxidoreductases, N-Demethylating / chemistry
  • Oxidoreductases, N-Demethylating / metabolism*
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary
  • Protein-Arginine Deiminase Type 4
  • Protein-Arginine Deiminases

Substances

  • Histones
  • Arginine
  • Oxidoreductases, N-Demethylating
  • Hydrolases
  • PADI4 protein, human
  • Protein-Arginine Deiminase Type 4
  • Protein-Arginine Deiminases
  • Lysine