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Structural and functional diversity of glutaredoxins in yeast

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Issue date
2010
Author
Herrero Perpiñán, Enrique
Bellí i Martínez, Gemma
Casas Herranz, Celia
Suggested citation
Herrero Perpiñán, Enrique; Bellí i Martínez, Gemma; Casas Herranz, Celia; . (2010) . Structural and functional diversity of glutaredoxins in yeast. Current protein & peptide science, 2010, vol. 11, núm. 8, p. 659-668. https://doi.org/10.2174/138920310794557637.
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Abstract
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 functional properties. Thus, dithiol glutaredoxins are able to reduce disulfide bonds and deglutathionylate mixed disulfides between glutathione and cysteine protein residues. They could act regulating the redox state of sulfhydryl residues of specific proteins, while thioredoxins (another family of thiol disulfide oxidoreductases which employ NADPH as electron donor) would be the general sulfhydryl reductants. Some dithiol glutaredoxins such as human Grx2 form dimers bridged by one iron-sulfur cluster, which acts as a sensor of oxidative stress, therefore regulating the activity of the glutaredoxin. The ability to interact with iron-sulfur clusters as ligands is also characteristic of monothiol glutaredoxins with a CGFS-type active site. These do not display thiol oxidoreductase activity, but have roles in iron homeostasis. The three members of this subfamily in Saccharomyces cerevisiae participate in the synthesis of the iron-sulfur clusters in mitochondria (Grx5), or in signalling the iron status inside the cell for regulation of iron uptake and intracellular iron relocalization (Grx3 and Grx4). Such role in iron metabolism seems to be evolutionary conserved. Fungal cells also contain membraneassociated glutaredoxins structurally and enzymatically similar to dithiol glutaredoxins, which may act as redox regulators at the early stages of the protein secretory machinery.
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http://hdl.handle.net/10459.1/47445
DOI
https://doi.org/10.2174/138920310794557637
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Current protein & peptide science, 2010, vol. 11, núm. 8, p. 659-668
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