Comprehending dynamic protein methylation with mass spectrometry

Curr Opin Chem Biol. 2013 Feb;17(1):12-9. doi: 10.1016/j.cbpa.2012.12.023. Epub 2013 Jan 18.

Abstract

Protein methylation is a post-translational modification (PTM) which modulates cellular and biological processes including transcription, RNA processing, protein interactions and protein dynamics. Methylation, catalyzed by highly specific methyltransferase enzymes, occurs on several amino acids including arginine, lysine, histidine and dicarboxylic amino acids like glutamate. Mass spectrometry (MS)-based techniques continue to be the methods of choice for the study of protein PTMs. These approaches are powerful and sensitive tools that have been used to identify, quantify and characterize protein methylation. In addition, metabolic labeling strategies can be coupled to MS detection in order to measure dynamic and differential in vivo protein methylation rates. In this review, different applications of mass spectrometry technologies and methods to study protein methylation are discussed.

Publication types

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

MeSH terms

  • Amino Acids / analysis
  • Amino Acids / metabolism
  • Animals
  • Histones / chemistry
  • Histones / metabolism
  • Humans
  • Mass Spectrometry / instrumentation
  • Mass Spectrometry / methods*
  • Methylation
  • Proteins / chemistry*
  • Proteins / metabolism

Substances

  • Amino Acids
  • Histones
  • Proteins