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A mass spectrometry based method for distinguishing between symmetrically and asymmetrically dimethylated arginine residues
Author(s) -
Brame Cynthia J.,
Moran Michael F.,
McBroomCerajewski Linda D. B.
Publication year - 2004
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1421
Subject(s) - chemistry , arginine , methylation , peptide , mass spectrometry , electrospray ionization , tandem mass spectrometry , dimethylamine , chromatography , protein arginine methyltransferase 5 , electrospray , ion , protein mass spectrometry , methyltransferase , biochemistry , amino acid , organic chemistry , gene
The arginine methylation of proteins is involved in several important cellular activities, most notably transcriptional control. Arginine dimethylation can take two distinct forms, symmetric and asymmetric, catalyzed by different classes of enzymes. To establish a method for the mass spectrometric identification and characterization of this post‐translational modification, we analyzed synthetic peptides with symmetrically or asymmetrically methylated arginine residues by electrospray ionization tandem mass spectrometry. We observed abundant characteristic ions at [M+nH–31] n+ and [M+nH–70] n+ in spectra of symmetrically methylated peptides and at [M+nH–45] n+ in spectra of asymmetrically methylated peptides. We speculate these ions arise from neutral loss of monomethylamine, dimethylcarbodiimide, and dimethylamine, respectively. These characteristic ions allowed the rapid identification of a symmetrically arginine‐dimethylated peptide from myelin basic protein and a symmetrically arginine‐dimethylated peptide from SmD3 co‐immunoprecipitated with the methyltransferase‐associated protein pICln, suggesting that this method may provide a rapid means to screen for and characterize dimethylarginine sites. Copyright © 2004 John Wiley & Sons, Ltd.