Histone methyltransferases

Histone methyltransferases are histone modifying enzymes that catalyze the transfer of one, two, or three methyl groups to the lysine and arginine residues of histones.  Histone methyltransferases act on the histone tails and the attachment of methyl groups occurs mainly at specific lysine or arginine residues on histones H3 and H4.  Histone methyltransferases are classified into two types: lysine methyltransferases, which are lysine specific, and arginine methyltransferases which are arginine specific.  In both types of histone methyltransferase, S-adenosyl methionine acts as a cofactor and the methyl donor group.  Arginine is usually mono- or dimethylated while lysine can be mono-, di-, or trimethylated.  Methylation of one or more of the amino acids within a histone tail leads to transcriptional silencing similar to that found with DNA methylation.  Mutations, genetic translocations and altered gene expression involving histone methyl transferases are frequently seen in cancer, developmental disorders and other pathologies.

Further reading

Yu and Zhuang (2019) Histone Methyltransferases as Therapeutic Targets for Kidney Diseases. Front Pharmacol. 10 1393 PMID: 31866860

Richart and Margueron (2020) Drugging histone methyltransferases in cancer. Curr Opin Chem Biol. 56 51 PMID: 31981999

Rugo et al (2020) The Promise for Histone Methyltransferase Inhibitors for Epigenetic Therapy in Clinical Oncology: A Narrative Review. Adv Ther. 37(7) 3059 PMID: 32445185