Title

Biochemical Analysis of Arginine Methylation in Transcription

Document Type

Book Chapter

Publication Date

12-1-2008

Journal

Methods in Molecular Biology Series

Volume

523

First Page

235

Last Page

247

URL with Digital Object Identifier

10.1007/978-1-59745-190-1_16

Abstract

Protein arginine methylation has emerged as an important mechanism for regulating the functions of proteins involved in diverse aspects of gene regulation such as transcriptional activation and repression, mRNA processing and nuclear-cytoplasmic shuttling. This modification is catalyzed by the PRMT family of enzymes which utilize intracellular S-adenosyl methionine as a cofactor to dimethylate-specific arginines found within many target proteins.The establishment of in vitro biochemical assays as well as the development of modification-specific antibodies, and more recently mass spectrometry, have increased our understanding of the mechanism of catalysis of the PRMT family of enzymes. In the following discussion, we present some of the more commonly used in vivo and in vitro techniques which can be utilized to study the mechanism of arginine methylation and its role in transcription.

Notes

Published as a book chapter in: Chromatin Protocols. (2nd ed.). Srikumar P. Chellappan. (Ed.).