Protein arginine methyltransferase 6 is a novel substrate of protein arginine methyltransferase 1  

作　　者：Meng-Tong Cao You Feng Y George Zheng 

机构地区：[1]Department of Pharmaceutical and Biomedical Sciences,University of Georgia,Athens,GA 30602,United States

出　　处：《World Journal of Biological Chemistry》2023年第5期84-98,共15页世界生物化学杂志（英文版）（电子版）

基　　金：Supported by National Institutes of Health,No.5R01GM126154 and No.1R35GM149230。

摘　　要：BACKGROUND Post-translational modifications play key roles in various biological processes.Protein arginine methyltransferases(PRMTs)transfer the methyl group to specific arginine residues.Both PRMT1 and PRMT6 have emerges as crucial factors in the development and progression of multiple cancer types.We posit that PRMT1 and PRMT6 might interplay directly or in-directly in multiple ways accounting for shared disease phenotypes.AIM To investigate the mechanism of the interaction between PRMT1 and PRMT6.METHODS Gel electrophoresis autoradiography was performed to test the methyltranferase activity of PRMTs and characterize the kinetics parameters of PRMTs.Liquid chromatography-tandem mass spectrometryanalysis was performed to detect the PRMT6 methylation sites.RESULTS In this study we investigated the interaction between PRMT1 and PRMT6,and PRMT6 was shown to be a novel substrate of PRMT1.We identified specific arginine residues of PRMT6 that are methylated by PRMT1,with R106 being the major methylation site.Combined biochemical and cellular data showed that PRMT1 downregulates the enzymatic activity of PRMT6 in histone H3 methylation.CONCLUSION PRMT6 is methylated by PRMT1 and R106 is a major methylation site induced by PRMT1.PRMT1 methylation suppresses the activity of PRMT6.

关 键 词：Posttranslational modification Arginine methylation Protein arginine methyltransferase 1 Protein arginine methyltransferase 6 CROSS-TALK Protein-protein interaction 

分 类 号：Q51[生物学—生物化学]