Grx5 Glutaredoxin Plays a Central Role in Protection against Protein Oxidative Damage in Saccharomyces cerevisiae
María Teresa Rodríguez-Manzaneque,Joaquim Ros,Elisa Cabiscol,Albert Sorribas,Enrique Herrero +4 more
TLDR
The synthetic lethality of the grx5 and grx2 mutations on one hand and ofgrx5 with thegrx3 grx4 combination on the other points to a complex functional relationship among yeast glutaredoxins, with Grx5 playing a specially important role in protection against oxidative stress both during ordinary growth conditions and after externally induced damage.Abstract:
Glutaredoxins are members of a superfamily of thiol disulfide oxidoreductases involved in maintaining the redox state of target proteins. In Saccharomyces cerevisiae, two glutaredoxins (Grx1 and Grx2) containing a cysteine pair at the active site had been characterized as protecting yeast cells against oxidative damage. In this work, another subfamily of yeast glutaredoxins (Grx3, Grx4, and Grx5) that differs from the first in containing a single cysteine residue at the putative active site is described. This trait is also characteristic for a number of glutaredoxins from bacteria to humans, with which the Grx3/4/5 group has extensive homology over two regions. Mutants lacking Grx5 are partially deficient in growth in rich and minimal media and also highly sensitive to oxidative damage caused by menadione and hydrogen peroxide. A significant increase in total protein carbonyl content is constitutively observed in grx5 cells, and a number of specific proteins, including transketolase, appear to be highly oxidized in this mutant. The synthetic lethality of the grx5 and grx2 mutations on one hand and of grx5 with the grx3 grx4 combination on the other points to a complex functional relationship among yeast glutaredoxins, with Grx5 playing a specially important role in protection against oxidative stress both during ordinary growth conditions and after externally induced damage. Grx5-deficient mutants are also sensitive to osmotic stress, which indicates a relationship between the two types of stress in yeast cells.read more
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Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
TL;DR: This comprehensive review summarizes fundamental principles of glutathione catalysis and compares the structures and mechanisms ofglutathione-dependent enzymes, including glutathion reductase, glutaredoxins, glutATHione peroxidases, peroxiredoxinases, glyoxalases 1 and 2, glutthione transferases and MAPEG.
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Thioredoxin and related molecules--from biology to health and disease.
TL;DR: Thioredoxin and binding proteins appear to control apoptosis or metabolic states such as carbohydrate and lipid metabolism related to diseases such as diabetes and atherosclerosis and the fundamental differences between bacterial and mammalian thiOREDoxin reductases offer new principles for treatment of infections.
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Roles of the Glutathione- and Thioredoxin-Dependent Reduction Systems in the Escherichia Coli and Saccharomyces Cerevisiae Responses to Oxidative Stress
Orna Carmel-Harel,Gisela Storz +1 more
TL;DR: The construction of strains carrying mutations in multiple genes is helping to elucidate the different roles of glutathione and thioredoxin, and studies with such strains have recently revealed that these two reduction systems modulate the activities of the E. coli OxyR and SoxR and the S. cerevisiae Yap1p transcriptional regulators of the adaptive responses to oxidative stress.
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Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system.
TL;DR: Glutaredoxins uniquely reduce mixed disulfides with glutathione via a monothiol mechanism where only an N-terminal low pKa Cys residue is required, by using their glutathionylation site.
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Stress‐controlled transcription factors, stress‐induced genes and stress tolerance in budding yeast
TL;DR: The possibility of using genetic approaches has made the yeast Saccharomyces cerevisiae a compelling model to study stress response at a molecular level and this information can be used to isolate and characterise stress-related proteins in higher eukaryotes and to design strategies to increase stress resistance in organisms of industrial interest.
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