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  • 1
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    Xylulose fermentation by mutant and wild-type strains of Zygosaccharomyces and Saccharomyces cerevisiae (2000)
    Springer
    Details
    Publication Date: 2000-04-12
    Print ISSN: 0175-7598
    Electronic ISSN: 1432-0614
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Springer
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  • 2
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    Herbicide-Induced Changes in Charge Recombination and Redox Potential of QA in the T4 Mutant of Blastochloris viridis (2005)
    American Chemical Society
    Details
    Publication Date: 2005-03-25
    Print ISSN: 0006-2960
    Electronic ISSN: 1520-4995
    Topics: Biology , Chemistry and Pharmacology
    Published by American Chemical Society
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  • 3
    Electronic Resource
    Electronic Resource
    Xylulose fermentation by mutant and wild-type strains of Zygosaccharomyces and Saccharomyces cerevisiae (2000)
    Springer
    Applied microbiology and biotechnology 53 (2000), S. 376-382 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Anaerobic xylulose fermentation was compared in strains of Zygosaccharomyces and Saccharomyces cerevisiae, mutants and wild-type strains to identify host-strain background and genetic modifications beneficial to xylose fermentation. Overexpression of the gene (XKS1) for the pentose phosphate pathway (PPP) enzyme xylulokinase (XK) increased the ethanol yield by almost 85% and resulted in ethanol yields [0.61 C-mmol (C-mmol consumed xylulose)−1] that were close to the theoretical yield [0.67 C-mmol (C-mmol consumed xylulose)−1]. Likewise, deletion of gluconate 6-phosphate dehydrogenase (gnd1Δ) in the PPP and deletion of trehalose 6-phosphate synthase (tps1Δ) together with trehalose 6-phosphate phosphatase (tps2Δ) increased the ethanol yield by 30% and 20%, respectively. Strains deleted in the promoter of the phosphoglucose isomerase gene (PGI1) – resulting in reduced enzyme activities – increased the ethanol yield by 15%. Deletion of ribulose 5-phosphate (rpe1Δ) in the PPP abolished ethanol formation completely. Among non-transformed and parental strains S. cerevisiae ENY. WA-1A exhibited the highest ethanol yield, 0.47 C-mmol (C-mmol consumed xylulose)−1. Other non-transformed strains produced mainly arabinitol or xylitol from xylulose under anaerobic conditions. Contrary to previous reports S. cerevisiae T23D and CBS 8066 were not isogenic with respect to pentose metabolism. Whereas, CBS 8066 has been reported to have a high ethanol yield on xylulose, 0.46 C-mmol (C-mmol consumed xylulose)−1 (Yu et al. 1995), T23D only formed ethanol with a yield of 0.24 C-mmol (C-mmol consumed xylulose)−1. Strains producing arabinitol did not produce xylitol and vice versa. However, overexpression of XKS1 shifted polyol formation from xylitol to arabinitol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051629
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  • 4
    Electronic Resource
    Electronic Resource
    Mutants that show increased sensitivity to hydrogen peroxide reveal an important role for the pentose phosphate pathway in protection of yeast against oxidative stress (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 456-464 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Oxidative stress ; Pentose phosphate pathway ; Ribulose 5-phosphate epimerase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have isolated several mutants ofSaccharomyces cerevisiae that are sensitive to oxidative stress in a screen for elevated sensitivity to hydrogen peroxide. Two of the sixteen complementation groups obtained correspond to structural genes encoding enzymes of the pentose phosphate pathway. Allelism of thepos10 mutation (POS forperoxidesensitivity) to thezwf1/met1 mutants in the structural gene for glucose 6-phosphate dehydrogenase was reported previously. The second mutation,pos18, was complemented by transformation with a yeast genomic library. The open reading frame of the isolated gene encodes 238 amino acids. No detectable ribulose 5-phosphate epimerase activity was found in thepos18 mutant, suggesting that the corresponding structural gene is affected in this mutant. For that reason the gene was renamedRPE1 (forribulose 5-phosphateepimerase).RPE1 was localized to chromosome X. The predicted protein has a molecular mass of 25 966 Daltons, a codon adaptation index (CAI) of 0.32, and an isoelectric point of 5.82. Database searches revealed 32 to 37% identity with ribulose 5-phosphate epimerases ofEscherichia coli, Rhodospirillum rubrum, Alcaligenes eutrophus andSolanum tuberosum. We have characterizedRPE1 by testing enzyme activities inrpe1 deletion mutants and in strains that overexpressRPE1, and compared the hydrogen peroxide sensitivity ofrpe1 mutants to that of other mutants in the pentose phosphate pathway. Interestingly, all mutants tested (glucose 6-phosphate dehydrogenase, gluconate 6-phosphate dehydrogenase, ribulose 5-phosphate epimerase, transketolase, transaldolase) are sensitive to hydrogen peroxide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02173011
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  • 5
    Electronic Resource
    Electronic Resource
    The oxidative stress response mediated via Pos9/Skn7 is negatively regulated by the Ras/PKA pathway in Saccharomyces cerevisiae (1999)
    Springer
    Molecular genetics and genomics 261 (1999), S. 740-752 
    Details
    ISSN: 1617-4623
    Keywords: Key words Oxidative stress ; Protein kinase A ; Msn2 ; Pos9 ; Yap1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Exposure of Saccharomyces cerevisiae to elevated concentrations of hydrogen peroxide induces transcription of several genes involved in the oxidative stress response. Two major transcription factors are involved in this induction, Pos9/Skn7 and Yap1. Fusions of either Yap1 or Pos9/Skn7 with the Gal4 DNA binding domain are active as transcription factors. Gal4-Yap1-dependent reporter gene activity is only weakly regulated by oxidative stress. In contrast, fusion of the Gal4 DNA binding domain to the Pos9/Skn7 protein results in a transcription factor that is independent of the YAP1 gene and is strictly regulated by oxidative stress, indicating that a signaling cascade impinges on the Pos9/Skn7 protein. We have observed that the Ras/PKA (cAMP-dependent protein kinase A) pathway affects this signaling. When PKA activity was low (in the presence of multicopy PDE2 or a cyr1 D822 → A mutation) maximum reporter gene activity was observed even in the absence of oxidative stress. In contrast, high PKA activity (in strains mutant for either pde2 or bcy1, or expressing the dominant active Ras2Val19) resulted in a complete loss of activation following oxidative stress. The transcription of Pos9/Skn7 target genes was also affected in Ras/PKA pathway mutants. Furthermore, we demonstrated that activated Pos9/Skn7 is necessary for Yap1-dependent reporter gene induction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050017
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  • 6
    Electronic Resource
    Electronic Resource
    The mitochondrial cytochrome c peroxidase Ccp1 of Saccharomyces cerevisiae is involved in conveying an oxidative stress signal to the transcription factor Pos9 (Skn7) (1999)
    Springer
    Molecular genetics and genomics 262 (1999), S. 437-447 
    Details
    ISSN: 1617-4623
    Keywords: Key words Oxidative stress signalling ; Mitochondria ; Pos9 (Skn7) ; Ccp1 ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In Saccharomyces cerevisiae two transcription factors, Pos9 (Skn7) and Yap1, are involved in the response to oxidative stress. Fusion of the Pos9 response-regulator domain to the Gal4 DNA-binding domain results in a transcription factor which renders the expression of a GAL1-lacZ reporter gene dependent on oxidative stress. To identify genes which are involved in the oxygen-dependent activation of the Gal4-Pos9 hybrid protein we screened for mutants that failed to induce the heterologous test system upon oxidative stress (fap mutants for factors activating Pos9). We isolated several respiration-deficient and some respiration-competent mutants by this means. We selected for further characterization only those mutants which also displayed an oxidative-stress-sensitive phenotype. One of the respiration-deficient mutants (complementation group fap6) could be complemented by the ISM1 gene, which encodes mitochondrial isoleucyl tRNA synthetase, suggesting that respiration competence was important for signalling of oxidative stress. In accordance with this notion a rho0 strain and a wild-type strain in which respiration had been blocked (by treatment with antimycin A or with cyanide) also failed to activate Gal4-Pos9 upon imposition of oxidative stress. Another mutant, fap24, which was respiration-competent, could be complemented by CCP1, which encodes the mitochondrial cytochrome c peroxidase. Mitochondrial cytochrome c peroxidase degrades reactive oxygen species within the mitochondria. This suggested a possible sensor function for the enzyme in the oxidative stress response. To test this we used the previously described point mutant ccp1 W191F , which is characterized by a 104-fold decrease in electron flux between cytochrome c and cytochrome c peroxidase. The Ccp1W191F mutant was still capable of activating the Pos9 transcriptional activation domain, suggesting that the signalling function of Ccp1 is independent of electron flux rates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380051103
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