Histone methylation in transcriptional control

Curr Opin Genet Dev. 2002 Apr;12(2):198-209. doi: 10.1016/s0959-437x(02)00287-3.

Abstract

Over the past year or so, methylation of histones has come to be recognised as a major player in the regulation of gene activity. This notion follows the discovery of lysine and arginine methyltransferases and proteins that recognise the methyl-lysine 'mark' on histones. Methylated histones have been implicated in heterochromatic repression, promoter regulation and the propagation of a repressed state via DNA methylation.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Gene Expression Regulation*
  • Histone-Lysine N-Methyltransferase / metabolism
  • Histones / genetics*
  • Histones / metabolism
  • Intracellular Signaling Peptides and Proteins
  • Methylation
  • Methyltransferases / genetics
  • Methyltransferases / metabolism
  • Molecular Sequence Data
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism
  • Protein Structure, Tertiary / genetics
  • Protein Structure, Tertiary / physiology
  • Protein-Arginine N-Methyltransferases
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Transcription Factors / genetics
  • Transcription Factors / metabolism
  • Transcription, Genetic*

Substances

  • DNA-Binding Proteins
  • Histones
  • Intracellular Signaling Peptides and Proteins
  • Nuclear Proteins
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Methyltransferases
  • Set2 protein, S cerevisiae
  • PRMT2 protein, human
  • Protein-Arginine N-Methyltransferases
  • Histone-Lysine N-Methyltransferase
  • PRDM2 protein, human
  • SET1 protein, S cerevisiae