Connecting the DOTs: covalent histone modifications and the formation of silent chromatin

Trends Genet. 2002 Aug;18(8):387-9. doi: 10.1016/s0168-9525(02)02746-4.


Histone methylation has emerged as a significant regulator of chromatin structure and function. Two different classes of histone methyltransferase (HMT) have been described, which target either lysine or arginine residues in the histone N-terminal tails. A flurry of recent papers now describe a third class of HMT that affects chromatin silencing indirectly, not by methylation of histone tails, but instead by targeting a conserved lysine residue in the core domain of the nucleosome.

Publication types

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

MeSH terms

  • Animals
  • Gene Silencing / physiology*
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase*
  • Histones / chemistry
  • Histones / physiology*
  • Humans
  • Methyltransferases / physiology*
  • Nuclear Proteins / physiology
  • Protein Methyltransferases
  • Saccharomyces cerevisiae Proteins*


  • Histones
  • Nuclear Proteins
  • Saccharomyces cerevisiae Proteins
  • Histone Methyltransferases
  • Methyltransferases
  • Protein Methyltransferases
  • Dot1 protein, S cerevisiae
  • Histone-Lysine N-Methyltransferase