The Redox Proteome

• Type of Material: Article
• Authors: Young-Mi Go, Emory University; Dean P Jones, Emory University
• Language: English
• Date: 2013-09-13
• Publisher: American Society for Biochemistry and Molecular Biology
• Publication Version: Final Published Version
• Copyright Statement: © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
• License: Creative Commons Attribution 3.0 Unported
• Final Published Version (URL): http://www.jbc.org/content/288/37/26512
• Title of Journal or Parent Work: Journal of Biological Chemistry
• ISSN: 0021-9258
• Volume: 288
• Issue: 37
• Start Page: 26512
• End Page: 26520
• Grant/Funding Information: This is the seventh article in the Thematic Minireview Series on Redox-active Protein Modifications and Signaling.; This work was supported, in whole or in part, by National Institutes of Health Grants ES009047, HL113451, and AG038746.
• Keywords: Systems Biology; Redox Regulation; Glutathione; Thioredoxin; Thiol
• Research Categories: Health Sciences, General

Abstract

The redox proteome consists of reversible and irreversible covalent modifications that link redox metabolism to biologic structure and function. These modifications, especially of Cys, function at the molecular level in protein folding and maturation, catalytic activity, signaling, and macromolecular interactions and at the macroscopic level in control of secretion and cell shape. Interaction of the redox proteome with redox-active chemicals is central to macromolecular structure, regulation, and signaling during the life cycle and has a central role in the tolerance and adaptability to diet and environmental challenges.