Structural and functional diversity of glutaredoxins in yeast
MetadataShow full item record
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.
Is part ofCurrent protein & peptide science, 2010, vol. 11, núm. 8, p. 659-668
European research projects
Showing items related by title, author, creator and subject.
Prokaryotic and eukaryotic monothiol glutaredoxins are able to perform the functions of Grx5 in the biogenesis of Fe/S clusters in yeast mitochondria Molina Navarro, Maria Micaela; Casas Herranz, Celia; Piedrafita Llorens, Lídia; Bellí i Martínez, Gemma; Herrero Perpiñán, Enrique (Elsevier, 2003)The Saccharomyces cerevisiae monothiol glutare- doxin Grx5 participates in the mitochondrial biogenesis of iron–sulfur clusters. Grx5 homologues exist in organisms from bacteria to humans. Chicken (cGRX5) and human ...
Herrero Perpiñán, Enrique; Ros Salvador, Joaquim; Tamarit Sumalla, Jordi; Bellí i Martínez, Gemma (Springer, 2006)Glutaredoxins (GRXs) can be subdivided into two subfamilies: dithiol GRXs with the CPY/FC active site motif, and monothiol GRXs with the CGFS motif. Both subfamilies share a thioredoxin-fold structure. Monothiol GRXs exist ...
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 ...