PROTEIN ARGININE METHYLTRANSFERASES AND THEIR INFLUENCE ON EPIGENOME

Protein arginine methyltransferases (PRMTs) are a family of epigenetic enzymes that catalyze the transfer of a methyl group from S-adenosylmethionine to an arginine residue in histone tails or nonhistone proteins. Among the PRMT family there are nine enzymes named according to the numbering PRMT1 - PRMT9. Due to the course of the catalyzed reaction, arginine methyltransferases have been divided into three classes: I, II and III. The first stage of the reaction in all classes proceeds in the same way and consists in the production of monomethylarginine. In the second stage of the reaction is the methylation stage and is separate for each enzyme class: PRMT I catalyzes the formation of asynunetrically dimethylated arginine, PRMT II leads to the production of symmetrically dimethylated arginine, while PRMT III only allows the formation of monomethylarginine. The methylation reaction on histone tail arginine residues leads to a change in the chromatin architecture, thus controlling its transcriptional activity. Arginine methyltransferases control many cellular processes, including: cell growth, proliferation and differentiation; transcription; repair of DNA damage; RNA processing, signal transduction; modulate the functioning of the immune system and enable the maintenance of glucose homeostasis. Unfortunately, dysregulation of arginine methyltransferases may lead to abnormal methylation patterns. The consequence of this reaction is the malfunctioning of important signaling pathways in the cell, leading to the development of chronic diseases. In this study we have proved that abnormal levels of arginine methyltransferases are conducive to the occurrence of': diabetes, cardiovascular diseases, bronchial asthma and numerous malignant tumors.