Adaptation to hydrogen peroxide in Saccharomyces cerevisiae: The role of NADPH-generating systems and the SKN7 transcription factor

Ng, Chong-Han; Tan, Shi‐Xiong; Perrone, Gabriel G.; Thorpe, Geoffrey W.; Higgins, Vincent J.; Dawes, Ian W.

doi:10.1016/j.freeradbiomed.2007.12.008

Cited by 43 publications

(51 citation statements)

References 67 publications

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“…Our results showed that the role of Zwf1 in production of NADPH and oxidative stress resistance in C. neoformans is unlike that in other fungi. In S. cerevisiae, deletion of Zwf1 results in a slow-growth phenotype and methionine auxotrophy (35,47,62). In contrast, our C. neoformans zwf1⌬ strain had no growth phenotype on rich, minimal, or methionine-deficient media, nor was it sensitive to changes in temperature.…”

Section: Figmentioning

confidence: 68%

“…In the model yeast Saccharomyces cerevisiae, NADPH-generating systems, including the pentose phosphate pathway, are critical for the ability of this organism to resist and adapt to high levels of oxidative stress (35,47). It has also been shown that the cytosolic copper/zinc superoxide dismutase and the pentose phosphate pathway have overlapping roles in protecting S. cerevisiae from oxidative stress and that both systems are critical for maintaining the intracellular redox state (62).…”

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confidence: 99%

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Isocitrate Dehydrogenase Is Important for Nitrosative Stress Resistance in Cryptococcus neoformans, but Oxidative Stress Resistance Is Not Dependent on Glucose-6-Phosphate Dehydrogenase

et al. 2010

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The opportunistic intracellular fungal pathogen Cryptococcus neoformans depends on many antioxidant and denitrosylating proteins and pathways for virulence in the immunocompromised host. These include the glutathione and thioredoxin pathways, thiol peroxidase, cytochrome c peroxidase, and flavohemoglobin denitrosylase. All of these ultimately depend on NADPH for either catalytic activity or maintenance of a reduced, functional form. The need for NADPH during oxidative stress is well established in many systems, but a role in resistance to nitrosative stress has not been as well characterized. In this study we investigated the roles of two sources of NADPH, glucose-6-phosphate dehydrogenase (Zwf1) and NADP ؉ -dependent isocitrate dehydrogenase (Idp1), in production of NADPH and resistance to oxidative and nitrosative stress. Deletion of ZWF1 in C. neoformans did not result in an oxidative stress sensitivity phenotype or changes in the amount of NADPH produced during oxidative stress compared to those for the wild type. Deletion of IDP1 resulted in greater sensitivity to nitrosative stress than to oxidative stress. The amount of NADPH increased 2-fold over that in the wild type during nitrosative stress, and yet the idp1⌬ strain accumulated more mitochondrial damage than the wild type during nitrosative stress. This is the first report of the importance of Idp1 and NADPH for nitrosative stress resistance.

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Section: Figmentioning

confidence: 68%

mentioning

confidence: 99%

Isocitrate Dehydrogenase Is Important for Nitrosative Stress Resistance in Cryptococcus neoformans, but Oxidative Stress Resistance Is Not Dependent on Glucose-6-Phosphate Dehydrogenase

et al. 2010

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“…Although the mechanisms responsible for this effect are not clear, several explanations can be given. It is known that hydrogen peroxide indirectly provokes a decrease of the NADPH pool, which is necessary for thiol reduction [12,[21][22][23]. The NADP + / NADPH ratio plays a critical role in the maintenance of redox homeostasis and its change may act as a signal for either SoxR oxidation or reduction.…”

Section: Regulation Of Global Responsementioning

confidence: 99%

“…The control of H 2 O 2 -adaptive response in S. cerevisiae involves Yap1p, Skn7p and Msn2p/Msn4p (Msn2/4p) transcriptional factors ( Figure 2) [7,23,26,32,33]. Mutants deleted for YAP1 or SKN7 as well as MSN2 and MSN4 genes were found to be unable to induce most antioxidant proteins of the H 2 O 2 stimulon, indicating that they were hypersensitive to hydrogen peroxide [55][56][57][58].…”

Section: Regulation Of Global Responsementioning

confidence: 99%

Hydrogen peroxide-induced response in E. coli and S. cerevisiae: different stages of the flow of the genetic information

Semchyshyn

2009

Open Life Sciences

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Adaptation to oxidative stress is a major topic in basic and applied research. Cell response to stressful changes is realized through coordinated reorganization of gene expression. E. coli and S. cerevisiae are extremely amenable to genetic or molecular biological and biochemical approaches, which make these microorganisms suitable models to study stress response at a molecular level in prokaryotes and eukaryotes, respectively. The main focus of this review is (i) to discuss transcriptional control of global response to hydrogen peroxide in E. coli and S. cerevisiae, (ii) to summarize recent literature data on E. coli and S. cerevisiae adaptive response to oxidative stress at different stages of the flow of the genetic information: from transcription and translation to functionally active proteins and (iii) to discuss possible reasons for a lack of correlation between the expression of certain antioxidant genes at different levels of cellular organization.

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“…The contribution of the Trr1p/Trx1,2p system is likely to become more important when cells experience certain stress conditions (e.g. oxidative) where the burden on the glutathione redox system is known to increase and GSSG overaccumulation may ensue (7,8,14,15). The observations that: 1) the gsh1 glr1 mutant can utilize GSSG as the sole source of glutathione; 2) the gsh1 glr1 strain accumulates GSH when challenged with exogenous GSSG and that overexpression of thioredoxins or thioredoxin reductase can reduce GSSG accumulation in glr1 cells; and 3) deletion of a single thioredoxin reduces the accumulation of GSH in the presence of excess GSSG all provide further support that the thioredoxin-thioredoxin reductase system can function to reduce GSSG to GSH in vivo.…”

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confidence: 99%

The Thioredoxin-Thioredoxin Reductase System Can Function in Vivo as an Alternative System to Reduce Oxidized Glutathione in Saccharomyces cerevisiae

Tan

Greetham

Raeth

et al. 2010

Journal of Biological Chemistry

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Cellular mechanisms that maintain redox homeostasis are crucial, providing buffering against oxidative stress. Glutathione, the most abundant low molecular weight thiol, is considered the major cellular redox buffer in most cells. To better understand how cells maintain glutathione redox homeostasis, cells of Saccharomyces cerevisiae were treated with extracellular oxidized glutathione (GSSG), and the effect on intracellular reduced glutathione (GSH) and GSSG were monitored over time. Intriguingly cells lacking GLR1 encoding the GSSG reductase in S. cerevisiae accumulated increased levels of GSH via a mechanism independent of the GSH biosynthetic pathway. Furthermore, residual NADPH-dependent GSSG reductase activity was found in lysate derived from glr1 cell. The cytosolic thioredoxin-thioredoxin reductase system and not the glutaredoxins (Grx1p, Grx2p, Grx6p, and Grx7p) contributes to the reduction of GSSG. Overexpression of the thioredoxins TRX1 or TRX2 in glr1 cells reduced GSSG accumulation, increased GSH levels, and reduced cellular glutathione E h . Conversely, deletion of TRX1 or TRX2 in the glr1 strain led to increased accumulation of GSSG, reduced GSH levels, and increased cellular E h . Furthermore, it was found that purified thioredoxins can reduce GSSG to GSH in the presence of thioredoxin reductase and NADPH in a reconstituted in vitro system. Collectively, these data indicate that the thioredoxin-thioredoxin reductase system can function as an alternative system to reduce GSSG in S. cerevisiae in vivo.

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Adaptation to hydrogen peroxide in Saccharomyces cerevisiae: The role of NADPH-generating systems and the SKN7 transcription factor

Cited by 43 publications

References 67 publications

Isocitrate Dehydrogenase Is Important for Nitrosative Stress Resistance in Cryptococcus neoformans, but Oxidative Stress Resistance Is Not Dependent on Glucose-6-Phosphate Dehydrogenase

Isocitrate Dehydrogenase Is Important for Nitrosative Stress Resistance in Cryptococcus neoformans, but Oxidative Stress Resistance Is Not Dependent on Glucose-6-Phosphate Dehydrogenase

Hydrogen peroxide-induced response in E. coli and S. cerevisiae: different stages of the flow of the genetic information

The Thioredoxin-Thioredoxin Reductase System Can Function in Vivo as an Alternative System to Reduce Oxidized Glutathione in Saccharomyces cerevisiae

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