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Submitted on August 29, 2003
Revised on September 26, 2003
Accepted on October 7, 2003

A proteomic analysis of arginine methylated protein complexes

François-Michel Boisvert, Jocelyn Côté, Marie-Chloé Boulanger, and Stéphane ;Richard

Departments of Oncology and Medicine, McHill University, Montreal, Quebec H3T1E2

Corresponding Author: stephane.richard{at}mcgill.ca

Arginine methylation is a post-translational modification that results in the formation of asymmetrical and symmetrical dimethylated arginines (aDMA, sDMA). This modification is catalyzed by type I and II protein arginine methyltransferases (PRMT), respectively. The two major enzymes PRMT1 (type I) and PRMT5 (type II) preferentially methylate arginines located in RG-rich clusters. Arginine methylation is a common modification but the reagents for detecting this modification have been lacking. Thus less than 20 proteins have been identified in the last 40 years to contain dimethylated arginines. We have previously generated four arginine methyl-specific antibodies: ASYM24 and ASYM25 are specific for aDMA whereas SYM10 and SYM11 recognize sDMA. All these antibodies were generated by using peptides with aDMA or sDMA in the context of different RG-rich sequences. HeLa cell extracts were used to purify the protein complexes recognized by each of the four antibodies and the proteins were identified by microcapillary reverse-phase liquid chromatography coupled on line with electrospray ionization tandem mass spectrometry (LC-MS/ MS). The analysis of 2 tandem mass spectra for each methyl-specific antibody resulted in the identification of over 200 new proteins that are putatively arginine methylated. The major protein complexes that were purified include components required for pre-mRNA splicing, polyadenylation, transcription, signal transduction and the cytoskeleton and DNA repair. These findings provide a basis for the identification of the role of arginine methylation in many cellular processes.


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