Oxidative Stress Response in Yeast: Purification and Some Properties of Oxidative Stress-inducible Glucose-6-phosphate Dehydrogenase from<i>Hansenula mrakii</i>

Miki, Takeo; Tsujimoto, Yasuhiro; Miyase, Shinji; Sugiyama, Keiichi; Izawa, Shingo; Inoue, Yoshiharu; Kimura, Akira

doi:10.1271/bbb.60.966

Cited by 11 publications

(9 citation statements)

References 5 publications

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“…A similar role for G6PDH in recycling the GSH pool has been suggested for yeast exposed to oxidative stress (Tran et al. , 1995; Miki et al. , 1996).…”

Section: Discussionsupporting

confidence: 65%

“…2h), so it is reasonable to assume that, in this lichen, the oxidative pentose shunt provided enough NADPH for rapid reduction of GSSG to GSH, which reached the level of controls after only 5 min. A similar role for G6PDH in recycling the GSH pool has been suggested for yeast exposed to oxidative stress (Tran et al, 1995;Miki et al, 1996). Interestingly, in an electrophoretic study, Gaff (1997) noted a new band of G6PDH activity in extracts from drying leaves of the resurrection grass Sporobolus stapfianus.…”

Section: Rehydration In Liquid Watermentioning

confidence: 57%

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Glutathione status correlates with different degrees of desiccation tolerance in three lichens

Kranner

2002

New Phytologist

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Summary• Glutathione-related mechanisms of coping with desiccation were studied in three lichens ( Pseudevernia furfuracea, Peltigera polydactyla and Lobaria pulmonaria ) with different degrees of tolerance. Reduced (GSH) and oxidised glutathione (GSSG), glutathione reductase (GR) and glucose-6-phosphate dehydrogenase (G6PDH) were measured during short-and long-term desiccation, and subsequent rehydration.• Glutathione was analysed by HPLC, and enzymes by spectrophotometry. Lichens were desiccated over silica gel, and rehydrated either in liquid water or water vapour.• Desiccation caused oxidation of almost all of the GSH. After short-term desiccation, rehydration caused rapid reduction of GSSG in all three species. Following longterm desiccation, P. furfuracea (the most desiccation-tolerant lichen studied) rapidly increased GSH when rehydrated in liquid water or water vapour. However, in P. polydactyla , neither method of rehydration re-established the initial GSH pool. After long-term desiccation, L. pulmonaria regenerated initial concentrations of GSH only when rehydrated in liquid water.• Reduction of GSSG was correlated with re-establishment of the predesiccation activity of G6PDH, a key enzyme of the oxidative pentose shunt. This enzyme probably provides NADPH during the first stages of rehydration, when photosynthesis is not yet possible.

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“…A similar role for G6PDH in recycling the GSH pool has been suggested for yeast exposed to oxidative stress (Tran et al. , 1995; Miki et al. , 1996).…”

Section: Discussionsupporting

confidence: 65%

Section: Rehydration In Liquid Watermentioning

confidence: 57%

Glutathione status correlates with different degrees of desiccation tolerance in three lichens

Kranner

2002

New Phytologist

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“…B, glutathione reductase (GR) activity. One unit of the activity was defined as the amount of enzyme reducing 1 mol of glutathione disulfide per min at 25°C as described in our previous paper (61). C, ␤-galactosidase activity derived from the GSH1-lacZ reporter gene.…”

Section: Fig 8 Effect Of Tsa1 Null Mutation On Glutathione Metabolismmentioning

confidence: 99%

Genetic Analysis of Glutathione Peroxidase in Oxidative Stress Response of Saccharomyces cerevisiae

Inoue

Matsuda

Sugiyama

et al. 1999

Journal of Biological Chemistry

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251

221

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Three glutathione peroxidase homologs (YKL026C, YBR244W, and YIR037W/HYR1) were found in the Saccharomyces Genome Database. We named them GPX1, GPX2, and GPX3, respectively, and we investigated the function of each gene product. The gpx3⌬ mutant was hypersensitive to peroxides, whereas null mutants of the GPX1 and GPX2 did not show any obvious phenotypes. Glutathione peroxidase activity decreased approximately 57 and 93% in the gpx3⌬ and gpx1⌬/gpx2⌬/ gpx3⌬ mutants, respectively, compared with that of wild type. Expression of the GPX3 gene was not induced by any stresses tested, whereas that of the GPX1 gene was induced by glucose starvation. The GPX2 gene expression was induced by oxidative stress, which was dependent upon the Yap1p. The TSA1 (thiol-specific antioxidant) gene encodes thioredoxin peroxidase that can reduce peroxides by using thioredoxin as a reducing power. Disruption of the TSA1 gene enhanced the basal expression level of the Yap1p target genes such as GSH1, GLR1, and GPX2 and that resulted in increases of total glutathione level and activities of glutathione reductase and glutathione peroxidase. However, expression of the TSA1 gene did not increase in the gpx1⌬/gpx2⌬/gpx3⌬ mutant. Therefore, de novo synthesis and recycling of glutathione were increased in the tsa1⌬ mutant to maintain the catalytic cycle of glutathione peroxidase reaction efficiently as a backup system for thioredoxin peroxidase.All aerobic organisms use molecular oxygen for respiration or oxidation of nutrients to acquire the energy efficiently. Molecular oxygen is reduced to H 2 O through acceptance of four electrons. During the reduction of molecular oxygen, several reactive oxygen species are formed, i.e. acceptance of one, two, and three electrons to form, respectively, superoxide anion radical (O 2 . ), hydrogen peroxide (H 2 O 2 ), and hydroxyl radical (HO ⅐ ). These reactive oxygen species attack almost all cell components, DNA, protein, and lipid membrane, and they sometimes cause lethal damage to the cells. Among the reactive oxygen species, HO ⅐ as well as perhydroxyl radical (HOO ⅐ ) can extract bis-allylic hydrogen atom of unsaturated fatty acid (LH) to form lipid alkyl radical (L ⅐ ) (1). The L ⅐ is oxidized by molecular oxygen to generate a lipid peroxy radical (LOO ⅐ ), and the LOO ⅐ thus formed reacts with LH to give lipid hydroperoxide (LOOH) and L ⅐ . A radical chain reaction is then propagated. LOOH also belongs to the reactive oxygen species, and the occurrence of the LOOHs in biological membranes may be one of the major oxidative damages to the cells. (2). ␤-Carotene and tocopherol function as radical scavengers. Glutathione is also a major antioxidant in aerobic cells. However, it has been widely believed that microorganisms do not have peroxidases whose electron donor is glutathione. Microorganisms are believed to use cytochrome c as an electron donor for the peroxidase reaction (cytochrome c peroxidase). GPx has been thought to be evolutionarily acquired by mammals. However, we have demonstrated that ...

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“…9,[16][17][18] Cyanobacterial G6PDHs seems to form oligomers (from dimer to tetramer,ˆnally to hexamer), leading to higher activity. 37) Likewise, in Chlorella the formation of the octamer might occur during hardening, leading to the activation of G6PDH2, although the reason for the activation of G6PDH2 during hardening remains unclear.…”

Section: Resultsmentioning

confidence: 99%

“…4,[11][12][13][14][15] Desiccation or oxidative stress, which are often associated with chilling, also tend to increase G6PDH activity in yeast, plants, and human cells. [16][17][18] Under a condition of cold hardening, to Downloaded by [Umeå University Library] at 14:17 09 October 2014 which glycolysis is sensitive, 12) increased activity of G6PDH may provide sustainable levels of NADPH to meet the biosynthetic events within the cells. 15,19,20) An increased NADPH level is also essential to maintain su‹cient reduced glutathione, which serves as antioxidant to detoxify H2O2 within cells under oxidative stress.…”

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confidence: 99%

Purification and Characterization of Two Isoforms of Glucose 6-Phosphate Dehydrogenase (G6PDH) fromChlorella vulgarisC-27

Honjoh¹,

Mimura²,

Kuroiwa³

et al. 2003

Bioscience, Biotechnology, and Biochemistry

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Two kinds of isoforms of glucose 6-phosphate dehydrogenase (G6PDH) were purified from cells of a freezing-tolerant strain, Chlorella vulgaris C-27, by sequential steps of chromatography on five kinds of columns, including a HiTrap Blue column which showed excellent separation of the isoforms from each other. The two isoforms (G6PDH1 and G6PDH2) were purified up to 109-fold and 197-fold with specific activity of 14.4 and 26.0 U/mg-protein, respectively. G6PDH1 showed an apparent Mr of 200,000 with a subunit Mr of about 58,000, whereas G6PDH2 showed an apparent Mr of 450,000 with a subunit Mr of about 52,000. The kinetic parameters were measured and several enzymatic features of the isoforms, such as effects of metal ions on the enzyme activity, were clarified, which showed that the two isoforms were different from each other in many respects. Among the effective ions, Cd2+ showed marked stimulating effects on both isoforms. G6PDH1 and G6PDH2 seem to be a cytosolic and a chloroplastic type, respectively, as judged by their sensitivity to DTT, and also from the results of sequence similarity searches using their N-terminal and internal amino acid sequences.

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Oxidative Stress Response in Yeast: Purification and Some Properties of Oxidative Stress-inducible Glucose-6-phosphate Dehydrogenase fromHansenula mrakii

Cited by 11 publications

References 5 publications

Glutathione status correlates with different degrees of desiccation tolerance in three lichens

Glutathione status correlates with different degrees of desiccation tolerance in three lichens

Genetic Analysis of Glutathione Peroxidase in Oxidative Stress Response of Saccharomyces cerevisiae

Purification and Characterization of Two Isoforms of Glucose 6-Phosphate Dehydrogenase (G6PDH) fromChlorella vulgarisC-27

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