Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions

@article{Grant2001RoleOT,
  title={Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions},
  author={Chris M. Grant},
  journal={Molecular Microbiology},
  year={2001},
  volume={39}
}
  • C. Grant
  • Published 2001
  • Biology, Medicine
  • Molecular Microbiology
Sulphydryl groups (‐SH) play a remarkably broad range of roles in the cell, and the redox status of cysteine residues can affect both the structure and the function of numerous enzymes, receptors and transcription factors. The intracellular milieu is usually a reducing environment as a result of high concentrations of the low‐molecular‐weight thiol glutathione (GSH). However, reactive oxygen species (ROS), which are the products of normal aerobic metabolism, as well as naturally occurring free… Expand
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References

SHOWING 1-10 OF 70 REFERENCES
Synthesis and role of glutathione in protection against oxidative stress in yeast.
  • C. Grant, I. Dawes
  • Biology, Medicine
  • Redox report : communications in free radical research
  • 1996
TLDR
Findings in the lower eukaryote Saccharomyces cerevisiae indicate that GSH is an essential metabolite in yeast, and that it is required for protection against oxidative stress produced by mitochondrial metabolism and exogenous reactive oxygen species. Expand
Grx5 Glutaredoxin Plays a Central Role in Protection against Protein Oxidative Damage inSaccharomyces cerevisiae
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. Expand
Yeast glutathione reductase is required for protection against oxidative stress and is a target gene for yAP‐1 transcriptional regulation
TLDR
Yeast mutants deleted for GLR1, encoding glutathione reductase, lack GLR activity and accumulate increased levels of GSSG, indicating a requirement forGLR in protection against oxidative stress. Expand
Metabolism and functions of glutathione in micro-organisms.
TLDR
GSH plays an important role in cellular protection during chemical stresses in spite of the fact that key enzymes of detoxification, such as GSH peroxidase and GSH S-transferase, remain at a low level. Expand
The Role of the Thioredoxin and Glutaredoxin Pathways in Reducing Protein Disulfide Bonds in the Escherichia coliCytoplasm*
TLDR
E. coli requires either a functional thioredoxin or glutaredoxin system to reduce disulfide bonds which appear after each catalytic cycle in the essential enzyme ribonucleotide reductase and perhaps to reduce non-native disulfides in cytoplasmic proteins. Expand
The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species.
TLDR
Grx1 and Grx2 function differently in the cell, and it is suggested that glutaredoxins may act as one of the primary defenses against mixed disulfides formed following oxidative damage to proteins. Expand
Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Saccharomyces cerevisiae.
TLDR
The idea that the two glutaredoxin isoforms in yeast play distinct roles during normal cellular growth and in response to stress conditions is supported. Expand
Thioredoxin-dependent peroxide reductase from yeast.
TLDR
The Saccharomyces cerevisiae thioredoxin reductase gene was also cloned and sequenced, and the deduced amino sequence was shown to be 51% identical with that of the Escherichia coli enzyme. Expand
Redox regulation of ubiquitin‐conjugating enzymes: mechanistic insights using the thiol‐specific oxidant diamide
  • M. Obin, F. Shang, Xin Gong, G. Handelman, J. Blumberg, Allen Taylor
  • Chemistry, Medicine
  • FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 1998
TLDR
S‐thiolation/dethiolation is supported as a mechanism regulating E1 and E2 activities in response to oxidant insult, and regulated by the GSSG:GSH ratio in a manner consistent with altered ubiquitin‐conjugating activity. Expand
Mitochondria of Saccharomyces cerevisiae Contain One-conserved Cysteine Type Peroxiredoxin with Thioredoxin Peroxidase Activity*
TLDR
It is shown that Prx1p, located in mitochondria, is overexpressed when cells use the respiratory pathway, as well as in response to oxidative stress conditions, and it has peroxide reductase activity in vitro using the yeast mitochondrial thioredoxin system as electron donor. Expand
...
1
2
3
4
5
...