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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. Symmetric dimethylation of histone H4 at arginine 3 (Arg3), catalyzed by the PRMT methyltransferases, is associated with transcriptional repression. Histone H4 dimethyl Arg3 symmetric methylation (H4R2me2s) is catalyzed by PRMT5 and PRMT7.
