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Screening of Substrates of protein arginine methyltransferase 1 in Glioma

Chinese Medical Sciences Journal 2012年第1期27卷 1-6页

作者： Shan Wang Xiao-chao Tan Bin Yang Bin Yin Xiao-zhong Peng National Laboratory of Medical Molecular Biology Institute of Basic Medical SciencesChinese Academy of Medical Sciences&Peking Union Medical CollegeBeijing 100005China

Objective To screen the asymmetric dimethyl arginines (ADMA)-containing proteins which could combine with protein arginine methyltransferase 1 (PRMT1). Methods Western blot was adopted to identify the expression of PRMT1 and the proteins with ADMA in glioma cell lines and normal brain tissues, and then to detect the changes of ADMA level after knock-down of PRMT1 with RNAi transfection in U87MG cells. Co-Immunoprecipitation (Co-IP), western blot, and sliver staining were employed to screen the candidate binding proteins of PRMT1. Then liquid chromatography-tandem mass spectrometry (LC-MS/MS) was used to identify the binding proteins of PRMT1. Results The expression of PRMT1 and some levels of ADMA were higher in glioma cell lines than in normal brain tissues. After knocking down PRMT1, some ADMA levels were found declined. After screening the binding proteins of PRMT1 with Co-IP and LC-MS/MS, 26 candidate binding proteins were identified. Among them, 6 candidate proteins had higher ions scores (>38) and bioinformation analysis predicted that SEC23-IP, ANKHD1-EIF4EBP3 protein, and 1-phosphatidylinositol-3-phosphate 5-kinase isoform 2 had possible methylated aginine sites. Conclusions The high expression of PRMT1 in glioma may induce the change of ADMA levels. Altogether 26 candidate proteins were identified, which contain ADMA and specifically bind with PRMT1.

关键词： protein arginine methyltransferase 1 asymmetric dimethyl arginines liquidchromatography-tandem mass spectrometry

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

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World Journal of Biological Chemistry 2023年第5期14卷 84-98页

作者： Meng-Tong Cao You Feng Y George Zheng Department of Pharmaceutical and Biomedical Sciences University of GeorgiaAthensGA 30602United States

BACKGROUND Post-translational modifications play key roles in various biological *** arginine methyltransferases(PRMTs)transfer the methyl group to specific arginine *** PRMT1 and PRMT6 have emerges as crucial factors in the development and progression of multiple cancer *** posit that PRMT1 and PRMT6 might interplay directly or in-directly in multiple ways accounting for shared disease *** To investigate the mechanism of the interaction between PRMT1 and *** Gel electrophoresis autoradiography was performed to test the methyltranferase activity of PRMTs and characterize the kinetics parameters of *** chromatography-tandem mass spectrometryanalysis was performed to detect the PRMT6 methylation *** In this study we investigated the interaction between PRMT1 and PRMT6,and PRMT6 was shown to be a novel substrate of *** identified specific arginine residues of PRMT6 that are methylated by PRMT1,with R106 being the major methylation *** biochemical and cellular data showed that PRMT1 downregulates the enzymatic activity of PRMT6 in histone H3 *** PRMT6 is methylated by PRMT1 and R106 is a major methylation site induced by ***1 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

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