Journal
FEBS LETTERS
Volume 581, Issue 19, Pages 3598-3607Publisher
WILEY
DOI: 10.1016/j.febslet.2007.07.002
Keywords
thiol redox control; thioredoxin; glutathione; oxidative stress; iron metabolism; ribonucleotide reductase
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By its ability to engage in a variety of redox reactions and coordinating metals, cysteine serves as a key residue in mediating enzymatic catalysis, protein oxidative folding and trafficking, and redox signaling. The thiol redox system, which consists of the glutathione and thioredoxin pathways, uses the cysteine residue to catalyze thiol-disulfide exchange reactions, thereby controlling the redox state of cytoplasmic cysteine residues and regulating the biological functions it subserves. Here, we consider the thiol redox systems of Escherichia coli and Saccharomyces cerevisiae, emphasizing the role of genetic approaches in the understanding of the cellular functions of these systems. We show that although prokaryotic and eukaryotic systems have a similar architecture, they profoundly differ in their overall cellular functions. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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