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Fe-S Proteins Acting as Redox Switch: New Key Actors of Cellular Adaptive Responses

Abstract : Iron-sulfur (Fe-S) clusters are inorganic prosthetic groups composed of only iron and inorganic sulfur atoms with variable nuclearities. Found in all kingdoms of life, they perform numerous critical functions in fundamental processes (e.g. respiration, photosynthesis, nitrogen fixation). Organisms develop different pathways to sense their local environment such as nutrient availability, level of oxida-tive stress or of an element such as iron, and to respond and adapt to changes. The chemistry of Fe-S clusters makes them ideal for sensing various redox environmental signals and subsequently for mediating appropriate cellular responses. Fe-S cluster-containing sensors can lose their cluster, accommodate another type of cluster (e.g. interconversion between 4Fe-4S and 2Fe-2S clusters) or receive/give electrons (change in the redox state of the cluster). The present review focuses on the latter sensing mechanism, which controls the activity of Fe-S proteins in response to redox signals by changing the redox state of its cluster. Proteins using this mechanism can be found in bacteria, yeasts as well as mammals and are involved in enzyme protection (FeSII), Fe-S cluster transfer/repair (mitoNEET), DNA repair (Base Excision Repair (BER) glycosylases and helicases), and regulation of gene expression (ThnY, AirS, SoxR). In all these proteins, when the Fe-S cluster is reduced, proteins are in a "dormant state". When their cluster perceives a signal that induces its oxidation, they switch to an "active state". This sensing mechanism efficiently helps cells to turn on survival pathways quickly and recover from stressful conditions.
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Submitted on : Wednesday, September 26, 2018 - 5:34:43 PM
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Marie-Pierre Golinelli-Cohen, Cécile Bouton. Fe-S Proteins Acting as Redox Switch: New Key Actors of Cellular Adaptive Responses. Current Chemical Biology, Bentham Science, 2017, 11 (2), pp.70-88. ⟨10.2174/2212796811666170406163809⟩. ⟨hal-01873512⟩

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