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 language | English |
|---|---|
| Pages (from-to) | 436-442 |
| Number of pages | 7 |
| Journal | Current Opinion in Structural Biology |
| Volume | 23 |
| Issue number | 3 |
| DOIs | |
| State | Published - 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.