Global analysis of posttranslational protein arginylation

PLoS Biol. 2007 Oct;5(10):e258. doi: 10.1371/journal.pbio.0050258.


Posttranslational arginylation is critical for embryogenesis, cardiovascular development, and angiogenesis, but its molecular effects and the identity of proteins arginylated in vivo are largely unknown. Here we report a global analysis of this modification on the protein level and identification of 43 proteins arginylated in vivo on highly specific sites. Our data demonstrate that unlike previously believed, arginylation can occur on any N-terminally exposed residue likely defined by a structural recognition motif on the protein surface, and that it preferentially affects a number of physiological systems, including cytoskeleton and primary metabolic pathways. The results of our study suggest that protein arginylation is a general mechanism for regulation of protein structure and function and outline the potential role of protein arginylation in cell metabolism and embryonic development.

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.

MeSH terms

  • Amino Acid Sequence
  • Aminoacyltransferases / deficiency
  • Aminoacyltransferases / genetics
  • Aminoacyltransferases / metabolism
  • Animals
  • Arginine / chemistry
  • Arginine / metabolism*
  • Cytoskeletal Proteins / metabolism
  • Gene Expression Regulation, Developmental*
  • Gene Silencing
  • Mice
  • Mice, Knockout
  • Molecular Sequence Data
  • Proteasome Endopeptidase Complex / metabolism*
  • Proteasome Inhibitors
  • Protein Processing, Post-Translational*
  • Proteins / metabolism*
  • Sequence Analysis, Protein


  • Cytoskeletal Proteins
  • Proteasome Inhibitors
  • Proteins
  • Arginine
  • Aminoacyltransferases
  • arginyltransferase
  • Proteasome Endopeptidase Complex