Dynamic protein methylation in chromatin biology

Cell Mol Life Sci. 2009 Feb;66(3):407-22. doi: 10.1007/s00018-008-8303-z.

Abstract

Post-translational modification of chromatin is emerging as an increasingly important regulator of chromosomal processes. In particular, histone lysine and arginine methylation play important roles in regulating transcription, maintaining genomic integrity, and contributing to epigenetic memory. Recently, the use of new approaches to analyse histone methylation, the generation of genetic model systems, and the ability to interrogate genome wide histone modification profiles has aided in defining how histone methylation contributes to these processes. Here we focus on the recent advances in our understanding of the histone methylation system and examine how dynamic histone methylation contributes to normal cellular function in mammals.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Arginine / metabolism
  • Chromatin / metabolism*
  • DNA Damage
  • Embryonic Stem Cells / physiology
  • Epigenesis, Genetic
  • Gene Expression Regulation
  • Germ Cells / physiology
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase
  • Histones / genetics
  • Histones / metabolism*
  • Lysine / metabolism
  • Methylation
  • Models, Molecular
  • Molecular Structure
  • Neoplasms / genetics
  • Neoplasms / metabolism
  • Oxidoreductases, N-Demethylating / genetics
  • Oxidoreductases, N-Demethylating / metabolism
  • Protein Conformation
  • Protein Methyltransferases / chemistry
  • Protein Methyltransferases / genetics
  • Protein Methyltransferases / metabolism
  • Protein Processing, Post-Translational*
  • Tumor Suppressor Protein p53 / genetics
  • Tumor Suppressor Protein p53 / metabolism

Substances

  • Chromatin
  • Histones
  • Tumor Suppressor Protein p53
  • Arginine
  • Oxidoreductases, N-Demethylating
  • Histone Methyltransferases
  • Protein Methyltransferases
  • Histone-Lysine N-Methyltransferase
  • Lysine