Monothiol glutaredoxins: a common domain for multiple functions
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Monothiol glutaredoxins with the CGFS sequence at the active site are widespread among prokaryotes and eukaryotes. Two subclasses exist, those with a single glutaredoxin domain and those with a thioredoxin-like region followed by one or more glutaredoxin domains. Studies in Saccharomyces cerevisiae
have demonstrated the role of the Grx5 protein in the biogenesis of iron-sulphur clusters. Grx5 homologues in other eukaryotes could carry out similar functions. Two S. cerevisiae monothiol glutaredoxins with the thioredoxin-like extension, Grx3 and Grx4, are modulators of the transcriptional activator Aft1, which regulates iron uptake in yeast. The human PICOT protein is a Grx3/Grx4 homologue with the same hybrid primary structure, which regulates protein kinase C activity and may participate in physiological processes such as control of cardiac function. Therefore, monothiol glutaredoxins share a common basic structural motif and biochemical mechanism of action, while participating in a diversity of cellular functions as protein redox regulators.
Is part ofCellular and molecular life sciences : CMLS, 2007, vol. 64, núm. 12, p. 1518-1530
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Herrero Perpiñán, Enrique; Bellí i Martínez, Gemma; Casas Herranz, Celia (Bentham Science Publishers, 2010)Glutaredoxins are defined as thiol disulfide oxidoreductases that reduce disulfide bonds employing reduced glutathione as electron donor. They constitute a complex family of proteins with a diversity of enzymatic and ...
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