Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 23, Issue 3, Pages 436-442Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2013.02.006
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Funding
- National Institutes of Health [RO1 GM065318]
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Cells are constantly exposed to various oxidants, either generated endogenously due to metabolic activity or excigenously. One way that cells respond to oxidants is through the action of redox-regulated proteins. These proteins also play important roles in oxidant signaling and protein biogenesis events. The key sensors built into redox-regulated proteins are cysteines, which undergo reversible thiol oxidation in response to changes in the oxidation status of the cellular environment. In this review, we discuss three examples of redox-regulated proteins found in bacteria, mitochondria, and chloroplasts. These proteins use oxidation of their redox-sensitive cysteines to reversibly convert large structural domains into more disordered regions or vice versa. These massive structural rearrangements are directly implicated in the functions of these proteins.
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