Histone arginine methylation and its dynamic regulation

Front Biosci. 2006 Jan 1;11:344-55. doi: 10.2741/1802.

Abstract

Methylation of histones by protein arginine methyltransferases (PRMTs) is increasingly being found to play an important and dynamic role in gene regulation. In mammals, PRMT1- and CARM1-catalyzed histone asymmetric dimethyl-arginine is involved in gene activation while PRMT5-catalyzed histone symmetric dimethyl-arginine is associated with gene repression. Insight into mechanisms by which histone arginine methylation can be dynamically regulated comes from recent reports demonstrating that conversion of histone methylarginine residues to citrulline by peptidylarginine deiminase 4 (PADI4) leads to transcriptional repression. While the downstream cellular effects of histone arginine methylation remain poorly understood, recent findings indicate that protein arginine methylation, in general, is required for mammalian development and is also likely important for cellular proliferation and differentiation. Given the surge of interest in histone arginine methylation, this review article will focus on recent progress in this area.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / chemistry
  • Amino Acid Sequence
  • Animals
  • Arginine / analogs & derivatives
  • Arginine / chemistry*
  • Catalysis
  • Cell Nucleus / metabolism
  • Gene Expression Regulation*
  • Histones / chemistry*
  • Humans
  • Hydrolases / chemistry
  • Methylation
  • Models, Biological
  • Molecular Sequence Data
  • Promoter Regions, Genetic
  • Protein Methyltransferases / metabolism
  • Protein-Arginine Deiminase Type 4
  • Protein-Arginine Deiminases
  • Protein-Arginine N-Methyltransferases / chemistry
  • Protein-Arginine N-Methyltransferases / metabolism
  • Signal Transduction
  • Transcription, Genetic
  • Transcriptional Activation

Substances

  • Histones
  • dimethylarginine
  • Adenosine Triphosphate
  • Arginine
  • Protein Methyltransferases
  • PRMT5 protein, human
  • Protein-Arginine N-Methyltransferases
  • coactivator-associated arginine methyltransferase 1
  • Hydrolases
  • PADI4 protein, human
  • Protein-Arginine Deiminase Type 4
  • Protein-Arginine Deiminases