[Progress in the study of histone methyltransferases]

Yi Chuan. 2007 Sep;29(9):1035-41. doi: 10.1360/yc-007-1035.
[Article in Chinese]

Abstract

Site- and state-specific lysine methylation of histones is catalyzed by a family of proteins including those contain the evolutionarily conserved SET domain. Research on histone methyltransferases is a part of epigenetics, which plays a fundamental role in heterochromatin formation, X-chromosome inactivation and transcription regulation. Aberrant histone methylation was linked to a number of developmental disorders and human disease including several carcinomas. Histone lysine methylation is a functionally complex process, as it can either activate or repress transcription, depending on sequence-specific lysine methylation site in histones. Non-histone proteins were found to be methylated by SET domain-containing histone methyltransferases whose primary targets were presumed to be histones. The researches on histone methyltransferases will make a completely new space for transcriptional activity, embryonic development, cell differentiation, and signal transduction.

Publication types

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

MeSH terms

  • Carcinoma / genetics
  • Carcinoma / metabolism
  • Carcinoma / pathology
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase
  • Histones / metabolism*
  • Humans
  • Methylation
  • Models, Biological
  • Protein Methyltransferases / chemistry
  • Protein Methyltransferases / genetics
  • Protein Methyltransferases / metabolism*
  • Protein Structure, Tertiary
  • Tumor Suppressor Protein p53 / metabolism

Substances

  • Histones
  • Tumor Suppressor Protein p53
  • Histone Methyltransferases
  • Protein Methyltransferases
  • Histone-Lysine N-Methyltransferase