کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1979135 1061661 2013 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
The roles of conditional disorder in redox proteins
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
The roles of conditional disorder in redox proteins
چکیده انگلیسی

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.


► Disulfide bond formation promotes large-scale order ⇔ disorder transitions.
► Redox-mediated unfolding of Hsp33 leads to its activation as chaperone.
► Redox-mediated folding of COX17 impacts its function as copper chaperone.
► Redox-mediated folding of CP12 makes it the ‘on–off’ switch of the Calvin cycle.
► Developments in structural techniques show promise in revealing protein disorder.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Current Opinion in Structural Biology - Volume 23, Issue 3, June 2013, Pages 436–442
نویسندگان
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