Open Access
Histone arginine methylation and its dynamic regulation
Joanna Wysocka1,C David Allis1,Scott Coonrod1
Laboratory of Chromatin Biology, Rockefeller University, New York, NY 10021, USA
DOI: 10.2741/1802 Volume 11 Issue 1, pp.344-355
Published: 01 January 2006
(This article belongs to the Special Issue Epigenetic effects during development and disease launch)

Methylation of histones by protein arginine methyltransferases (PRMTs) is increasingly being found to play an important and dynamic role in gene regulation. In mammals, PRMT1- and CARM1-catalyzed histone asymmetric dimethyl-arginine is involved in gene activation while PRMT5-catalyzed histone symmetric dimethyl-arginine is associated with gene repression. Insight into mechanisms by which histone arginine methylation can be dynamically regulated comes from recent reports demonstrating that conversion of histone methylarginine residues to citrulline by peptidylarginine deiminase 4 (PADI4) leads to transcriptional repression. While the downstream cellular effects of histone arginine methylation remain poorly understood, recent findings indicate that protein arginine methylation, in general, is required for mammalian development and is also likely important for cellular proliferation and differentiation. Given the surge of interest in histone arginine methylation, this review article will focus on recent progress in this area.

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Joanna Wysocka, C David Allis, Scott Coonrod. Histone arginine methylation and its dynamic regulation. Frontiers in Bioscience-Landmark. 2006. 11(1); 344-355.