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Updated: Feb 3, 2026

In vitro Methylation Assay to Study Protein Arginine Methylation
Published on: October 5, 2014
Development of Chaetocin and S-Adenosylmethionine Analogues as Tools for Studying Protein Methylation
Yoshihiro Sohtome1,2,3, Mikiko Sodeoka1,2,3
1Synthetic Organic Chemistry Laboratory, RIKEN Cluster for Pioneering Research, 2-1 Hirosawa, Wako, Saitama, Japan.
Abstract:
Physiological regulatory mechanisms of protein, RNA, and DNA functions include small chemical modifications, such as methylation, which are introduced or removed in a highly chemo-, regio-, and site-selective manner by methyltransferases and demethylases, respectively. However, mimicking or controlling these modifications by using labeling reagents and inhibitors remains challenging. In this Personal Account, we introduce our nascent interdisciplinary collaboration between chemists and biologists aimed at developing a basic strategy to analyse and control the methylation reactions regulated by protein methyltransferases (PMTs). We focus in particular on the structural development of chaetocin and S-adenosylmethionine to obtain PMT inhibitors and PMT substrate detectors.
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