The roles of conditional disorder in redox proteins

Dana Reichmann*, Ursula Jakob

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

39 Scopus citations

Abstract

Cells are constantly exposed to various oxidants, either generated endogenously due to metabolic activity or exogenously. 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.

Original languageAmerican English
Pages (from-to)436-442
Number of pages7
JournalCurrent Opinion in Structural Biology
Volume23
Issue number3
DOIs
StatePublished - Jun 2013

Bibliographical note

Funding Information:
We thank James Bardwell for critically reading this manuscript. This work was supported by a National Institutes of Health RO1 GM065318 award to U.J.

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