Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2003 Dec;2(12):1319-30.
doi: 10.1074/mcp.M300088-MCP200. Epub 2003 Oct 7.

A proteomic analysis of arginine-methylated protein complexes

François-Michel Boisvert  1 , Jocelyn Côté, Marie-Chloé Boulanger, Stéphane Richard
Affiliations
Free article

A proteomic analysis of arginine-methylated protein complexes

François-Michel Boisvert et al. Mol Cell Proteomics. 2003 Dec.
Free article

Abstract

Arginine methylation is a post-translational modification that results in the formation of asymmetrical and symmetrical dimethylated arginines (a- and 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, fewer than 20 proteins have been identified in the last 40 years as containing dimethylated arginines. We have generated previously four arginine methyl-specific antibodies; ASYM24 and ASYM25 are specific for aDMA, whereas SYM10 and SYM11 recognize sDMA. All of 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. The analysis of two 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 cytoskeleton and DNA repair. These findings provide a basis for the identification of the role of arginine methylation in many cellular processes.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

Publication types

LinkOut - more resources

-