Methods applied to the study of protein arginine methylation

Methods Enzymol. 2012;512:71-92. doi: 10.1016/B978-0-12-391940-3.00004-4.

Abstract

Arginine methylation was discovered in the mid-1960s. About 15 years ago, the first protein arginine N-methyltransferase (PRMT) enzyme was described. The PRMT family now stands at nine members, and these enzymes play a key role in regulating a multitude of cellular events. The majority of the PRMTs have been deleted in mice, thus providing genetically tractable systems for in vivo and cell-based studies. These studies have implicated this posttranslational modification in chromatin remodeling, transcriptional regulation, RNA processing, protein/RNA trafficking, signal transduction, and DNA repair. In this chapter, we introduce different approaches that have been developed to assess protein arginine methylation levels and characterize PRMT substrates.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Antibodies, Monoclonal, Murine-Derived / chemistry
  • Arginine / chemistry*
  • Cell Extracts / chemistry
  • DNA-Binding Proteins / chemistry
  • Enzyme Assays*
  • Enzyme Inhibitors / chemistry
  • Escherichia coli
  • Fibroblasts / enzymology
  • Gene Knockout Techniques
  • HeLa Cells
  • Humans
  • Methylation
  • Mice
  • Peptide Fragments / chemistry
  • Protein Processing, Post-Translational*
  • Protein-Arginine N-Methyltransferases / antagonists & inhibitors
  • Protein-Arginine N-Methyltransferases / biosynthesis
  • Protein-Arginine N-Methyltransferases / chemistry*
  • Protein-Arginine N-Methyltransferases / genetics
  • Rabbits
  • Recombinant Fusion Proteins / antagonists & inhibitors
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / chemistry*
  • Reticulocytes / enzymology

Substances

  • Antibodies, Monoclonal, Murine-Derived
  • Cell Extracts
  • DNA-Binding Proteins
  • Enzyme Inhibitors
  • Peptide Fragments
  • Recombinant Fusion Proteins
  • Arginine
  • Protein-Arginine N-Methyltransferases
  • coactivator-associated arginine methyltransferase 1