Development of Chaetocin and S‐Adenosylmethionine Analogues as Tools for Studying Protein Methylation. Issue 12 (16th October 2018)

• Record Type: Journal Article
• Authors: Sohtome, Yoshihiro; Sodeoka, Mikiko
• Is Part Of: Chemical record. Volume 18:Issue 12(2018)
• Page Start: 1660
• Page End: 1671
• Publication Date: 2018-10-16
• Subjects: protein methylation -- inhibitor -- epidithiodiketopiperazine -- detector -- proteomics; Chemistry -- Periodicals; 540
• DOI: 10.1002/tcr.201800118
• Languages: English
• ISSNs: 1527-8999

Abstract

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. Abstract : Protein methylation reaction controlled by protein methyltransferases (PMTs) is a mechanistic basis to control a wide variety of biological events. In this Personal Account, we will introduce our studies on exploring the PMT inhibitors and on chemical methylome analysis using a protein substrate detector.