Proteome‐Wide Survey of Cysteine Oxidation by Using a Norbornene Probe. (24th January 2020)

• Record Type: Journal Article
• Authors: Alcock, Lisa J.; Langini, Maike; Stühler, Kai; Remke, Marc; Perkins, Michael V.; Bernardes, Gonçalo J. L.; Chalker, Justin M.
• Is Part Of: Chembiochem. Volume 21:Number 9(2020)
• Page Start: 1329
• Page End: 1334
• Publication Date: 2020-01-24
• Subjects: cysteine oxidation -- norbornene -- oxidative stress -- sulfenic acid -- sulfenome; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201900729
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract: Rapid detection of cysteine oxidation in living cells is critical in advancing our understanding of responses to reactive oxygen species (ROS) and oxidative stress. Accordingly, there is a need to develop chemical probes that facilitate proteome‐wide detection of cysteine's many oxidation states. Herein, we report the first whole‐cell proteomics analysis using a norbornene probe to detect the initial product of cysteine oxidation: cysteine sulfenic acid. The oxidised proteins identified in the HeLa cell model represent the first targets of the ROS hydrogen peroxide. The panel of protein hits provides new and important information about the targets of oxidative stress, including 148 new protein members of the sulfenome. These findings provide new leads for the study and understanding of redox signalling and diseases associated with oxidative stress. Abstract : Acid test : A norbornene probe was used to survey protein oxidation in live cells by trapping the cysteine sulfenic acids generated during oxidative stress. Of the 482 proteins significantly enriched and sequenced in the assay, 148 have never been previously identified as members of the sulfenome.