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  • 1
    Electronic Resource
    Electronic Resource
    Role of cysteines in the activation and inactivation of brewers' yeast pyruvate decarboxylase investigated with a PDC1-PDC6 fusion protein (1993)
    s.l. : American Chemical Society
    Biochemistry 32 (1993), S. 2704-2709 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00061a031
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  • 2
    Electronic Resource
    Electronic Resource
    Substrate Activation of Brewers' Yeast Pyruvate Decarboxylase Is Abolished by Mutation of Cysteine 221 to Serine (1994)
    s.l. : American Chemical Society
    Biochemistry 33 (1994), S. 5630-5635 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00184a035
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular cloning of a gene involved in glucose sensing in the yeast Saccharomyces cerevisiae (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 8 (1993), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Cells of the yeast Saccharomyces cerevisiae display a wide range of glucose-induced regulatory phenomena, including glucose-induced activation of the RAS-adenylate cyclase pathway and phosphatidylinositol turnover, rapid post-translational effects on the activity of different enzymes as well as long-term effects at the transcriptional level. A gene called GGS1 (for General Glucose Sensor) that is apparently required for the glucose-induced regulatory effects and several ggs1 alleles (fdp1, byp1 and cif1) has been cloned and characterized. A GGS1 homologue is present in Methanobacterium thermoautotrophicum. Yeast ggs1 mutants are unable to grow on glucose or related readily fermentable sugars, apparently owing to unrestricted influx of sugar into glycolysis, resulting in its rapid deregulation. Levels of intracellular free glucose and metabolites measured over a period of a few minutes after addition of glucose to cells of a ggsi1Δ strain are consistent with our previous suggestion of a functional interaction between a sugar transporter, a sugar kinase and the GGS1 gene product. Such a glucose-sensing system might both restrict the influx of glucose and activate several signal transduction pathways, leading to the wide range of glucose-induced regulatory phenomena. Deregulation of these pathways in ggs1 mutants might explain phenotypic defects observed in the absence of glucose, e.g. the inability of ggs1 diploids to sporulate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1993.tb01638.x
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  • 4
    Electronic Resource
    Electronic Resource
    PDC6, a weakly expressed pyruvate decarboxylase gene from yeast, is activated when fused spontaneously under the control of the PDC1 promoter (1991)
    Springer
    Current genetics 20 (1991), S. 373-378 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; Pyruvate decarboxylase ; Gene expression ; Codon usage ; Gene fusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Three structural genes encode the pyruvate decarboxylase isoenzymes in the yeast Saccharomyces cerevisiae. PDC1 and PDC5 are active during glucose fermentation where PDC1 is expressed about six times more strongly than PDC5. Expression of PDC6 is weak and seems to be induced in ethanol medium. Consequently, pdc1Δ pdc5Δ double mutants do not ferment glucose and do not grow on glucose medium. Spontaneous mutants, derived from such a pdc1 pdc5 strain, were isolated which could again ferment glucose. They showed pyruvate decarboxylase activity due to a duplication of PDC6. The second copy of PDC6 was expressed under the control of the PDC1 promoter, which was still present in the pdc1 strain. However, the resulting PDC1-PDC6 fusion gene could only partially substitute for PDC1: to achieve normal growth and high pyruvate decarboxylase activity strains carrying PDC1-PDC6 required a functional PDC5 gene which is dispensable in a PDC1 wild-type background. Thus, expression of PDC5 depends on the state of the PDC1 locus: low in the PDC1 wild-type background and high in PDC1-PDC6 fusion strains and, as shown previously, in pdc1 mutants. The activation of PDC5 expression in PDC1-PDC6 strains may be due to particular properties of the PDC1-PDC6 fusion protein or simply to the weaker expression of PDC1-PDC6 in comparison to the wild-type PDC1 gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00317064
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  • 5
    Electronic Resource
    Electronic Resource
    The byp1-3 allele of the Saccharomyces cerevisiae GGS1/TPS1 gene and its multi-copy suppressor tRNAGLN (CAG): Ggs1/Tps1 protein levels restraining growth on fermentable sugars and trehalose accumulation (1994)
    Springer
    Current genetics 26 (1994), S. 295-301 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; Trehalose synthase ; GGS1/TPS1 gene ; Glycolysis ; Fermentable sugars ; Suppression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Byp1-3 is an amber nonsense allele of the Sacchromyces cerevisiae GGS1/TPS1 gene which encodes the small subunit of the trehalose synthase complex. Mutations in this gene confer an inability to grow on glucose or fructose but the phenotype of byp1-3 mutants is leaky in a strain-dependent manner. Overexpression of the isolated byp1-3 allele suppressed the growth defect of a ggs1/tps1Δ mutant. Expression of an in-vitro-generated mutant allele of GGS1/TPS1 that lacks all the coding sequences downstream from the byp1-3 mutation led to the production of a shortened protein that did not complement the ggs1/tps1Δ mutant. We have isolated, as an allele-specific multi-copy suppressor of the growth defect of the byp1-3 mutant on fructose, the gene for tRNAGLN (CAG). Thus the leaky phenotype of byp1-3 mutants is due to a low level of read through of the internal nonsense codon by tRNAGLN (CAG). Using overexpression of the isolated byp1-3 allele, as well as of the tRNAGLN (CAG) gene, we were able to demonstrate that as little as about 10% of the normal Ggs1/Tps1 protein level is sufficient for slow growth on fructose. We also show a correlation between the level of Ggs1/Tps1, the ability to accumulate trehalose in stationary phase and the ability to grow on fermentable sugars. Sequence analysis of the cloned tRNAGLN (CAG) gene showed that it is located 700 bp upstream of URA10. However, we found considerable differences to the reported sequence of URA10, in particular in the non-coding region.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00310492
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  • 6
    Electronic Resource
    Electronic Resource
    Characterization of the osmotic-stress response inSaccharomyces cerevisiae: osmotic stress and glucose repression regulate glycerol-3-phosphate dehydrogenase independently (1994)
    Springer
    Current genetics 25 (1994), S. 12-18 
    Details
    ISSN: 1432-0983
    Keywords: Osmotic stress ; Glycerol ; Glycerol-3-phosphate dehydrogenase ; Glucose repression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Micro-organisms have developed systems to adapt to sudden changes in the environment. Here we describe the response of the yeastSaccharomyces cerevisiae to osmotic stress. A drop in the water activity (aw) of the medium following the addition of NaCl led to an immediate shrinkage of the cells. During the 2 h following the osmotic shock the cells partially restored their cell volume. This process depended on active protein synthesis. During the recovery period the cells accumulated glycerol intracellularly as a compatible solute and very little glycerol was leaking out of the cell. We have investigated in more detail the enzymes of glycerol metabolism and found that only the cytoplasmic glycerol-3-phosphate dehydrogenase was strongly induced. The level of induction was dependent on the yeast strain used and the degree of osmotic stress. The synthesis of cytoplasmic glycerol-3-phosphate dehydrogenase is also regulated by glucose repression. Using mutants defective in glucose repression (hxk2Δ), or derepression (snf1Δ), and with invertase as a marker enzyme, we show that glucose repression and the osmotic-stress response system regulate glycerol-3-phosphate dehydrogenase synthesis independently. We infer that specific control mechanisms sense the osmotic situation of the cell and induce responses such as the production and retention of glycerol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00712960
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  • 7
    Electronic Resource
    Electronic Resource
    The growth and signalling defects of the ggs1 (fdp1/byp1) deletion mutant on glucose are suppressed by a deletion of the gene encoding hexokinase PII (1993)
    Springer
    Current genetics 23 (1993), S. 281-289 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; Glycolysis ; Glucose sensor ; Hexokinase ; Trehalose ; Signalling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Yeast cells defective in the GGS1 (FDP1/BYP1) gene are unable to adapt to fermentative metabolism. When glucose is added to derepressed ggs1 cells, growth is arrested due to an overloading of glycolysis with sugar phosphates which eventually leads to a depletion of phosphate in the cytosol. Ggs1 mutants lack all glucose-induced regulatory effects investigated so far. We reduced hexokinase activity in ggs1 strains by deleting the gene HXK2 encoding hexokinase PII. The double mutant ggs1Δ, hxk2Δ grew on glucose. This is in agreement with the idea that an inability of the ggs1 mutants to regulate the initiation of glycolysis causes the growth deficiency. However, the ggs1Δ, hxk2Δ double mutant still displayed a high level of glucose-6-phosphate as well as the rapid appearance of free intracellular glucose. This is consistent with our previous model suggesting an involvement of GGS1 in transport-associated sugar phosphorylation. Glucose induction of pyruvate decarboxylase, glucoseinduced cAMP-signalling, glucose-induced inactivation of fructose-1,6-bisphosphatase, and glucose-induced activation of the potassium transport system, all deficient in ggs1 mutants, were restored by the delection of HXK2. However, both the ggs1Δ and the ggs1Δ, hk2Δ mutant lack detectable trehalose and trehalose-6-phosphate synthase activity. Trehalose is undetectable even in ggs1Δ strains with strongly reduced activity of protein kinase A which normally causes a very high trehalose content. These data fit with the recent cloning of GGS1 as a subunit of the trehalose-6-phosphate synthase/phosphatase complex. We discuss a possible requirement of trehalose synthesis for a metabolic balance of sugar phosphates and free inorganic phosphate during the transition from derepressed to fermentative metabolism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00310888
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  • 8
    Electronic Resource
    Electronic Resource
    Characterisation of PDC2, a gene necessary for high level expression of pyruvate decarboxylase structural genes in Saccharomyces cerevlsiae (1993)
    Springer
    Molecular genetics and genomics 241 (1993), S. 657-666 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Pyruvate decarboxylase ; Transcription ; Glucose induction ; Autoregulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The regulatory gene PDC2 was identified in a screen for mutations affecting pyruvate decarboxylase activity in yeast. I have cloned and sequenced this gene. The predicted protein of 925 amino acids has no homology to any sequence in the databases. However, the protein sequence is rich in asparagine and serine residues, as is often found for transcriptional regulators. The PDC2 deletion mutant exhibits a phenotype very similar to, but more severe than that of the point mutant: a strongly reduced pyruvate decarboxylase specific activity, slow, respiration-dependent growth on glucose, and accumulation of pyruvate. The activity of other glycolytic enzymes seems to be unaffected by the pdc2Δ mutation. Synthesis of pyruvate decarboxylase is regulated by PDC2 at the transcriptional level. Expression of the major structural gene for pyruvate decarboxylase, PDC1, is strongly reduced in pdc2Δ mutants. Transcription of the generally more weakly expressed PDC5 gene appears to be entirely abolished. However, glucose induction of pyruvate decarboxylase synthesis is unaffected. Thus, PDC2 is either important for a high basal level of PDC gene expression or it plays a positive role in the autoregulation that controls expression of PDC1 and PDC5.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00279908
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