Arginine methylation is a broadly expressed post-translational modification (PTM) that occurs on both nuclear and cytoplasmic proteins. It is especially prevalent on proteins that can shuttle continuously between the nucleus and the cytoplasm.
Arginine can be mono-methylated or di-methylated. There are two main types of arginine di-methylation: asymmetric (two methyl groups on the same nitrogen within the arginine residue side chain) and symmetric (each methyl group on a separate nitrogen). For example, symmetric di-methylation of histone H3 at arginine 2 (H3R2me2s) is associated with active chromatin, whereas histone H4R3me2s is linked to heterochromatin formation and silencing of genes.
The methylation of histone arginine is catalyzed by a family of enzymes called protein arginine methyltransferases (PRMTs), of which there are three main types. Type I (e.g., CARM1, PRMT1, PRMT2, PRMT3, PRMT6, and PRMT8) and type II (e.g., PRMT5 and PRMT9) are responsible for the asymmetric and symmetric di-methylation of arginine residues, respectively, as well as for mono-methylation, while type III (e.g., PRMT7) produces only mono-methylated arginine.
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