The roles of conditional disorder in redox proteins

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• 作者：Dana Reichmann¹ ; ^{danare@mail.huji.ac.il} ; Ursula Jakob² ; ³ ; ^{ujakob@umich.edu}
• 刊名：Current Opinion in Structural Biology
• 出版年：2013
• 出版时间：June, 2013
• 年：2013
• 卷：23
• 期：3
• 页码：436-442
• 全文大小：682 K

文摘

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.