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We are analyzing https://link.springer.com/article/10.1007/bf00311211.

Title:
Mutants of Saccharomyces cerevisiae sensitive to oxidative and osmotic stress | Current Genetics
Description:
Although oxidative stress is involved in many human diseases, little is known of its molecular basis in eukaryotes. In a genetic approach, S. cerevisiae was used to identify elements involved in oxidative stress. By using hydrogen peroxide as an agent for oxidative stress, 34 mutants were identified. All mutants were recessive and fell into 16 complementation groups (pos1 to pos16 for peroxide sensitivity). They corresponded to single mutations as shown by a 2:2 segregation pattern. Enzymes reportedly involved in oxidative stress, such as glucose-6-phosphate dehydrogenase, glutathione reductase, superoxide dismutase, as well as glutathione concentrations, were investigated in wild-type and mutant-cells. One complementation group lacked glucose-6-phosphate dehydrogenase and was shown to be allelic to the glucose-6-phosphate dehydrogenase structural gene ZWF1/MET19. In other mutants all enzymes supposedly involved in oxidative-stress resistance were still present. However, several mutants showed strongly elevated levels of glutathione reductase, gluconate-6-phosphate dehydrogenase and glucose-6-phosphate dehydrogenase. One complementation group, pos9, was highly sensitive to oxidative stress and revealed the same growth phenotype as the previously described yap1/par1 mutant coding for the yeast homologue of mammalian transcriptional activator protein, c-Jun, of the proto-oncogenic AP-1 complex. However, unlike par1 mutants, which showed diminished activities of oxidative-stress enzymes and glutathion level, the pos9 mutants did not reveal any such changes. In contrast to other recombinants between pos mutations and par1, the sensitivity did not further increase in par1 pos9 recombinants, which may indicate that both mutations belong to the same regulating circuit. Interestingly, ten complementation groups were, in parallel, sensitive to osmotic stress, and one mutant allele revealed increased heat sensitivity. Our results indicate that a surprisingly large number of genes seem to be involved in oxidative-stress resistance and a possible overlap exists between osmotic stress and other stress reactions.
Website Age:
28 years and 1 months (reg. 1997-05-29).

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  • Education
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Custom-built

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🌠 Phenomenal Traffic: 5M - 10M visitors per month


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How Does Link.springer.com Make Money? {💸}

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Keywords {🔍}

google, scholar, gene, cerevisiae, saccharomyces, yeast, stress, biochem, oxidative, superoxide, article, mutants, dismutase, dehydrogenase, cell, involved, protein, biol, oxygen, pos, glucosephosphate, mol, sequence, eur, transcription, privacy, cookies, content, osmotic, entian, mutations, resistance, par, access, proc, sci, usa, expression, science, characterization, information, publish, search, genetics, sensitive, krems, genetic, complementation, natl, acad,

Topics {✒️}

month download article/chapter encoding glucose-6-phosphate dehydrogenase gamma-glutamylcysteine synthetase gene rieske iron-sulphur protein nf-kb transcription factor saccharomyces cerevisiae ctt1-gene proto-oncogenic ap-1 complex copper-dependent transcription factor zinc-superoxide dismutase gene yap1/par1 mutant coding nuclear gene coding moye-rowley ws glucose-6-phosphate dehydrogenase privacy choices/manage cookies metallothionein gene expression yeast nuclear gene saccharomyces cerevisiae gene gluconate-6-phosphate dehydrogenase showed diminished activities full article pdf amplified genetic locus zinc superoxide dismutase yeast metallothionein expression mothercell specific transcription yeast saccharomyces cerevisiae superoxide dismutase activity saccharomyces cerevisiae sensitive high-copy number manganese superoxide dismutase transcription factor involved oxidative-stress resistance yeast ho gene european economic area scope submit manuscript surprisingly large number heatshock transeription factors mammalian uv response functionally unrelated chemicals marie-curie-strasse 9 ten complementation groups oxidative-stress enzymes oxidative stress responses c-jun gene yeast gene expression conditions privacy policy hydroxyl radical generated transcriptional activator proteins gene previously assumed reduce ethanol tolerance deduced aminoacid sequence

Questions {❓}

  • Bilinski T, Krawiec Z, Liczmanski A, Litwinska J (1985) Is hydroxyl radical generated by the Fenton chemistry?

Schema {🗺️}

WebPage:
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         headline:Mutants of Saccharomyces cerevisiae sensitive to oxidative and osmotic stress
         description:Although oxidative stress is involved in many human diseases, little is known of its molecular basis in eukaryotes. In a genetic approach, S. cerevisiae was used to identify elements involved in oxidative stress. By using hydrogen peroxide as an agent for oxidative stress, 34 mutants were identified. All mutants were recessive and fell into 16 complementation groups (pos1 to pos16 for peroxide sensitivity). They corresponded to single mutations as shown by a 2:2 segregation pattern. Enzymes reportedly involved in oxidative stress, such as glucose-6-phosphate dehydrogenase, glutathione reductase, superoxide dismutase, as well as glutathione concentrations, were investigated in wild-type and mutant-cells. One complementation group lacked glucose-6-phosphate dehydrogenase and was shown to be allelic to the glucose-6-phosphate dehydrogenase structural gene ZWF1/MET19. In other mutants all enzymes supposedly involved in oxidative-stress resistance were still present. However, several mutants showed strongly elevated levels of glutathione reductase, gluconate-6-phosphate dehydrogenase and glucose-6-phosphate dehydrogenase. One complementation group, pos9, was highly sensitive to oxidative stress and revealed the same growth phenotype as the previously described yap1/par1 mutant coding for the yeast homologue of mammalian transcriptional activator protein, c-Jun, of the proto-oncogenic AP-1 complex. However, unlike par1 mutants, which showed diminished activities of oxidative-stress enzymes and glutathion level, the pos9 mutants did not reveal any such changes. In contrast to other recombinants between pos mutations and par1, the sensitivity did not further increase in par1 pos9 recombinants, which may indicate that both mutations belong to the same regulating circuit. Interestingly, ten complementation groups were, in parallel, sensitive to osmotic stress, and one mutant allele revealed increased heat sensitivity. Our results indicate that a surprisingly large number of genes seem to be involved in oxidative-stress resistance and a possible overlap exists between osmotic stress and other stress reactions.
         datePublished:
         dateModified:
         pageStart:427
         pageEnd:434
         sameAs:https://doi.org/10.1007/BF00311211
         keywords:
             Saccharomyces cerevisiae
            Oxidative stress
            Osmotic stress
            Microbial Genetics and Genomics
            Microbiology
            Biochemistry
            general
            Cell Biology
            Plant Sciences
            Proteomics
         image:
         isPartOf:
            name:Current Genetics
            issn:
               1432-0983
               0172-8083
            volumeNumber:27
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               Periodical
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      headline:Mutants of Saccharomyces cerevisiae sensitive to oxidative and osmotic stress
      description:Although oxidative stress is involved in many human diseases, little is known of its molecular basis in eukaryotes. In a genetic approach, S. cerevisiae was used to identify elements involved in oxidative stress. By using hydrogen peroxide as an agent for oxidative stress, 34 mutants were identified. All mutants were recessive and fell into 16 complementation groups (pos1 to pos16 for peroxide sensitivity). They corresponded to single mutations as shown by a 2:2 segregation pattern. Enzymes reportedly involved in oxidative stress, such as glucose-6-phosphate dehydrogenase, glutathione reductase, superoxide dismutase, as well as glutathione concentrations, were investigated in wild-type and mutant-cells. One complementation group lacked glucose-6-phosphate dehydrogenase and was shown to be allelic to the glucose-6-phosphate dehydrogenase structural gene ZWF1/MET19. In other mutants all enzymes supposedly involved in oxidative-stress resistance were still present. However, several mutants showed strongly elevated levels of glutathione reductase, gluconate-6-phosphate dehydrogenase and glucose-6-phosphate dehydrogenase. One complementation group, pos9, was highly sensitive to oxidative stress and revealed the same growth phenotype as the previously described yap1/par1 mutant coding for the yeast homologue of mammalian transcriptional activator protein, c-Jun, of the proto-oncogenic AP-1 complex. However, unlike par1 mutants, which showed diminished activities of oxidative-stress enzymes and glutathion level, the pos9 mutants did not reveal any such changes. In contrast to other recombinants between pos mutations and par1, the sensitivity did not further increase in par1 pos9 recombinants, which may indicate that both mutations belong to the same regulating circuit. Interestingly, ten complementation groups were, in parallel, sensitive to osmotic stress, and one mutant allele revealed increased heat sensitivity. Our results indicate that a surprisingly large number of genes seem to be involved in oxidative-stress resistance and a possible overlap exists between osmotic stress and other stress reactions.
      datePublished:
      dateModified:
      pageStart:427
      pageEnd:434
      sameAs:https://doi.org/10.1007/BF00311211
      keywords:
          Saccharomyces cerevisiae
         Oxidative stress
         Osmotic stress
         Microbial Genetics and Genomics
         Microbiology
         Biochemistry
         general
         Cell Biology
         Plant Sciences
         Proteomics
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            1432-0983
            0172-8083
         volumeNumber:27
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            Periodical
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         name:Springer-Verlag
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            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
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                     name:Institut für Mikrobiologie, Frankfurt/Main, Germany
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