The roles of conditional disorder in redox proteins
By Dana Reichmann, Ursula Jakob. 2013
51 citations recorded by the source corpus.
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.
Subfields: Cell Biology, Inorganic Chemistry, Molecular Biology
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In Cell Biology
In Molecular Biology
- Gábor Erdös
- Zsuzsanna Dosztányi
- Bálint Mészáros
- Vladimir N Uversky
- Lukasz Kurgan
- Fanchi Meng
- Zhenling Peng
- Jörg Gsponer
Citations in the corpus
- IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding (2018, background): “An important category in this class corresponds to redox potential regulated proteins that play important roles in oxidant signalling and protein biogenesis events (37).”