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Updated: May 19, 2026

In vitro Methylation Assay to Study Protein Arginine Methylation
Published on: October 5, 2014
Methods applied to the study of protein arginine methylation
Donghang Cheng1, Vidyasiri Vemulapalli, Mark T Bedford
1Department of Molecular Carcinogenesis, The University of Texas MD Anderson Cancer Center, Smithville, Texas, USA. dcheng@mdanderson.org
Abstract:
Arginine methylation was discovered in the mid-1960s. About 15 years ago, the first protein arginine N-methyltransferase (PRMT) enzyme was described. The PRMT family now stands at nine members, and these enzymes play a key role in regulating a multitude of cellular events. The majority of the PRMTs have been deleted in mice, thus providing genetically tractable systems for in vivo and cell-based studies. These studies have implicated this posttranslational modification in chromatin remodeling, transcriptional regulation, RNA processing, protein/RNA trafficking, signal transduction, and DNA repair. In this chapter, we introduce different approaches that have been developed to assess protein arginine methylation levels and characterize PRMT substrates.

