Glutathione reductase from Brassica rapa affects tolerance and the redox state but not fermentation ability in response to oxidative stress in genetically modified Saccharomyces cerevisiae

Arsenite [As(III)] is a highly toxic chemical to all organisms. Previously, we reported that the overexpression of NtCyc07 enhanced As(III) tolerance and reduced As(III) accumulation in yeast (Saccharomyces cerevisiae) and tobacco (Nicotiana tabacum). To understand a mechanism for higher As(III) tolerance and lower As(III) accumulation in NtCyc07-overexpressing tobacco, we examined the expression levels of various putative As(III) transporters (aquaporin). The expressions of putative As(III) exporter NIP1;1, PIP1;1, 1;5, 2;1, 2;2, and 2;7 were enhanced, while the expressions of putative As(III) importer NIP3;1, 4;1, and XIP2;1 were decreased, contributing to the reduced accumulation of As(III) in NtCyc07-overexpressing tobacco. In addition, the levels of oxidative stress indicators (H2O2, superoxide and malondialdehyde) were lower, and the activities of antioxidant enzymes (catalase, superoxide dismutase and glutathione reductase) were higher in NtCyc07-tobacco than in the control tobacco. This suggests that the lower oxidative stress in transgenic tobacco may be attributed to the higher activities of antioxidant enzymes and lower As(III) levels. Taken together, the overexpression of NtCyc07 enhances As(III) tolerance by reducing As(III) accumulation through modulation of expressions of putative As(III) transporters in tobacco.

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Overlapping Roles of the Cytoplasmic and Mitochondrial Redox Regulatory Systems in the Yeast Saccharomyces cerevisiae

Eukaryotic Cell ◽

10.1128/ec.4.2.392-400.2005 ◽

2005 ◽

Vol 4 (2) ◽

pp. 392-400 ◽

Cited By ~ 60

Author(s):

Eleanor W. Trotter ◽

Chris M. Grant

Keyword(s):

Oxidative Stress ◽

Saccharomyces Cerevisiae ◽

Redox State ◽

Redox Homeostasis ◽

Thioredoxin Reductase ◽

Normal Growth ◽

Growth Conditions ◽

Reduced Form ◽

Yeast Saccharomyces Cerevisiae ◽

Thioredoxin System

ABSTRACT Thioredoxins are small, highly conserved oxidoreductases which are required to maintain the redox homeostasis of the cell. Saccharomyces cerevisiae contains a cytoplasmic thioredoxin system (TRX1, TRX2, and TRR1) as well as a complete mitochondrial thioredoxin system, comprising a thioredoxin (TRX3) and a thioredoxin reductase (TRR2). In the present study we have analyzed the functional overlap between the two systems. By constructing mutant strains with deletions of both the mitochondrial and cytoplasmic systems (trr1 trr2 and trx1 trx2 trx3), we show that cells can survive in the absence of both systems. Analysis of the redox state of the cytoplasmic thioredoxins reveals that they are maintained independently of the mitochondrial system. Similarly, analysis of the redox state of Trx3 reveals that it is maintained in the reduced form in wild-type cells and in mutants lacking components of the cytoplasmic thioredoxin system (trx1 trx2 or trr1). Surprisingly, the redox state of Trx3 is also unaffected by the loss of the mitochondrial thioredoxin reductase (trr2) and is largely maintained in the reduced form unless cells are exposed to an oxidative stress. Since glutathione reductase (Glr1) has been shown to colocalize to the cytoplasm and mitochondria, we examined whether loss of GLR1 influences the redox state of Trx3. During normal growth conditions, deletion of TRR2 and GLR1 was found to result in partial oxidation of Trx3, indicating that both Trr2 and Glr1 are required to maintain the redox state of Trx3. The oxidation of Trx3 in this double mutant is even more pronounced during oxidative stress or respiratory growth conditions. Taken together, these data indicate that Glr1 and Trr2 have an overlapping function in the mitochondria.

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Faculty Opinions recommendation of Mitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiae.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1009153.119858 ◽

2002 ◽

Author(s):

Thomas Nystrom

Keyword(s):

Oxidative Stress ◽

Saccharomyces Cerevisiae ◽

Labile Iron Pool ◽

Labile Iron ◽

Iron Pool

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Idebenone Treatment Mediates the Effect of Menadione Oxidative Stress Damage in Saccharomyces cerevisiae

Drug Metabolism Letters ◽

10.2174/1872312811206020120 ◽

2012 ◽

Vol 6 (2) ◽

pp. 120-123 ◽

Cited By ~ 2

Author(s):

Oliver Gamondi ◽

Sebastian Chapela ◽

Ines Nievas ◽

Isabel Burgos ◽

Manuel Alonso ◽

...

Keyword(s):

Oxidative Stress ◽

Saccharomyces Cerevisiae ◽

Stress Damage

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Imaging NAD(H) Redox Alterations in Cryopreserved Alveolar Macrophages from Ozone-Exposed Mice and the Impact of Nutrient Starvation during Long Lag Times

Antioxidants ◽

10.3390/antiox10050767 ◽

2021 ◽

Vol 10 (5) ◽

pp. 767

Author(s):

He N. Xu ◽

Joanna Floros ◽

Lin Z. Li ◽

Shaili Amatya

Keyword(s):

Oxidative Stress ◽

Alveolar Macrophages ◽

Redox State ◽

Redox Status ◽

Nutrient Starvation ◽

Ozone Exposure ◽

Reduced Form ◽

Time Period ◽

Lag Times ◽

The Impact

Employing the optical redox imaging technique, we previously identified a significant redox shift of nicotinamide adenine dinucleotide (NAD and the reduced form NADH) in freshly isolated alveolar macrophages (AM) from ozone-exposed mice. The goal here was twofold: (a) to determine the NAD(H) redox shift in cryopreserved AM isolated from ozone-exposed mice and (b) to investigate whether there is a difference in the redox status between cryopreserved and freshly isolated AM. We found: (i) AM from ozone-exposed mice were in a more oxidized redox state compared to that from filtered air (FA)-exposed mice, consistent with the results obtained from freshly isolated mouse AM; (ii) under FA exposure, there was no significant NAD(H) redox difference between fresh AM that had been placed on ice for 2.5 h and cryopreserved AM; however, under ozone exposure, fresh AM were more oxidized than cryopreserved AM; (iii) via the use of nutrient starvation and replenishment and H2O2-induced oxidative stress of an AM cell line, we showed that this redox difference between cryopreserved and freshly isolated AM is likely the result of the double “hit”, i.e., the ozone-induced oxidative stress plus nutrient starvation that prevented freshly isolated AM from a full recovery after being on ice for a prolonged time period. The cryopreservation technique we developed eliminates/minimizes the effects of oxidative stress and nutrient starvation on cells. This method can be adopted to preserve lung macrophages from animal models or clinical patients for further investigations.

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Serum Albumin Redox States: More than Oxidative Stress Biomarker

Antioxidants ◽

10.3390/antiox10040503 ◽

2021 ◽

Vol 10 (4) ◽

pp. 503

Author(s):

Fuka Tabata ◽

Yasuaki Wada ◽

Satomi Kawakami ◽

Kazuhiro Miyaji

Keyword(s):

Oxidative Stress ◽

Serum Albumin ◽

Animal Studies ◽

Redox State ◽

Ex Vivo ◽

Pathological Condition ◽

Analytical Techniques ◽

Cysteine Residue ◽

Research Field ◽

Systemic Oxidative Stress

Serum albumin is the most abundant circulating protein in mammals including humans. It has three isoforms according to the redox state of the free cysteine residue at position 34, named as mercaptalbumin (reduced albumin), non-mercaptalbumin-1 and -2 (oxidized albumin), respectively. The serum albumin redox state has long been viewed as a biomarker of systemic oxidative stress, as the redox state shifts to a more oxidized state in response to the severity of the pathological condition in various diseases such as liver diseases and renal failures. However, recent ex vivo studies revealed oxidized albumin per se could aggravate the pathological conditions. Furthermore, the possibility of the serum albumin redox state as a sensitive protein nutrition biomarker has also been demonstrated in a series of animal studies. A paradigm shift is thus ongoing in the research field of the serum albumin. This article provides an updated overview of analytical techniques for serum albumin redox state and its association with human health, focusing on recent findings.

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A manganese oxide nanozyme prevents the oxidative damage of biomolecules without affecting the endogenous antioxidant system

Nanoscale ◽

10.1039/c8nr09397k ◽

2019 ◽

Vol 11 (9) ◽

pp. 3855-3863 ◽

Cited By ~ 22

Author(s):

Namrata Singh ◽

Mohammed Azharuddin Savanur ◽

Shubhi Srivastava ◽

Patrick D'Silva ◽

Govindasamy Mugesh

Keyword(s):

Oxidative Stress ◽

Oxidative Damage ◽

Manganese Oxide ◽

Antioxidant System ◽

Mammalian Cells ◽

Redox State ◽

Stress Conditions ◽

System P ◽

Endogenous Antioxidant ◽

Antioxidant Machinery

Multi-enzyme mimetic Mn3O4 nanoflowers (Mp) modulate the redox state of mammalian cells without altering the cellular antioxidant machinery under oxidative stress conditions.

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