Plant PRMTs broaden the scope of arginine methylation

J Genet Genomics. 2012 May 20;39(5):195-208. doi: 10.1016/j.jgg.2012.04.001. Epub 2012 Apr 11.

Abstract

Post-translational methylation at arginine residues is one of the most important covalent modifications of proteins, involved in a myriad of essential cellular processes in eukaryotes, such as transcriptional regulation, RNA processing, signal transduction, and DNA repair. Methylation at arginine residues is catalyzed by a family of enzymes called protein arginine methyltransferases (PRMTs). PRMTs have been extensively studied in various taxa and there is a growing tendency to unveil their functional importance in plants. Recent studies in plants revealed that this evolutionarily conserved family of enzymes regulates essential traits including vegetative growth, flowering time, circadian cycle, and response to high medium salinity and ABA. In this review, we highlight recent advances in the field of post-translational arginine methylation with special emphasis on the roles and future prospects of this modification in plants.

Publication types

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

MeSH terms

  • Arginine / metabolism*
  • Gene Expression Regulation, Plant
  • Methylation
  • Multigene Family
  • Plant Development
  • Plant Proteins / genetics
  • Plant Proteins / metabolism*
  • Plants / enzymology*
  • Plants / genetics
  • Plants / metabolism
  • Protein-Arginine N-Methyltransferases / genetics
  • Protein-Arginine N-Methyltransferases / metabolism*

Substances

  • Plant Proteins
  • Arginine
  • Protein-Arginine N-Methyltransferases