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Background:Histone H4 is one of the core components of the nucleosome, the basic building block of chromatin. Histones are subject to a variety of chemical modifications, including post-translational modifications of the histone proteins and the methylation of cytosine residues in the DNA. Reported histone modifications include acetylation, methylation, phosphorylation, ubiquitylation, glycosylation, ADP-ribosylation, carbonylation and SUMOylation; these modifications play a major role in regulating gene expression. The methylation of histones can occur on two different residues: arginine or lysine. Asymmetric dimethylation of histone H4 at arginine 3 (Arg3), catalyzed by the PRMT methyltransferases, is associated with transcriptional activation by nuclear hormone receptors. Arg3 methylation has been reported to facilitate the subsequent acetylation of histone H4 by the acetyltransferase p300. Histone H4 dimethyl Arg3 asymmetric methylation (H4R2me2a) is catalyzed by PRMT1 and PRMT6.
