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 ...
Saccharomyces cerevisiae Grx6 and Grx7 are monothiol glutaredoxins associated with the early secretory pathway Izquierdo Álvarez, Alicia; Casas Herranz, Celia; Mühlenhoff, Ulrich; Lillig, Christopher Horst; Herrero Perpiñán, Enrique (American Society for Microbiology, 2008)Saccharomyces cerevisiae Grx6 and Grx7 are two monothiol glutaredoxins whose active-site sequences (CSYS and CPYS, respectively) are reminiscent of the CPYC active-site sequence of classical dithiol glutaredoxins. Both ...
Izquierdo Álvarez, Alicia; Casas Herranz, Celia; Herrero Perpiñán, Enrique (Society for General Microbiology, 2010)Unlike in higher organisms, selenium is not essential for growth in Saccharomyces cerevisiae. In this species, it causes toxic effects at high concentrations. In the present study, we show that when supplied as selenite ...