Proteomic analysis of arginine methylation sites in human cells reveals dynamic regulation during transcriptional arrest.

ABSTRACT: The covalent attachment of methyl groups to the side-chain of arginine residues is known to play essential roles in regulation of transcription, protein function, and RNA metabolism. The specific N-methylation of arginine residues is catalyzed by a small family of gene products known as protein arginine methyltransferases; however, very little is known about which arginine residues become methylated on target substrates. Here we describe a proteomics methodology that combines single-step immunoenrichment of methylated peptides with high-resolution mass spectrometry to identify endogenous arginine mono-methylation (MMA) sites. We thereby identify 1027 site-specific MMA sites on 494 human proteins, discovering numerous novel mono-methylation targets and confirming the majority of currently k

SUBMITTER: Sylvestersen KB 

PROVIDER: S-EPMC4125738 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature