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  • Genetics  (1)
  • Hexokinase  (1)
  • Trehalose synthase  (1)
  • 1
    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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  • 2
    Electronic Resource
    Electronic Resource
    Control of glucose influx into glycolysis and pleiotropic effects studied in different isogenic sets of Saccharomyces cerevisiae mutants in trehalose biosynthesis (1995)
    Springer
    Current genetics 27 (1995), S. 110-122 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; Trehalose synthase ; GGS1/TPS1 gene ; Isogenic background ; Glucose transport ; Sporulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The GGS1/TPS1 gene of the yeast Saccharomyces cerevisiae encodes the trehalose-6-phosphate synthase subunit of the trehalose synthase complex. Mutants defective in GGS1/TPS1 have been isolated repeatedly and they showed variable pleiotropic phenotypes, in particular with respect to trehalose content, ability to grow on fermentable sugars, glucose-induced signaling and sporulation capacity. We have introduced the fdp1, cif1, byp1 and glc6 alleles and the ggs1/tps1 deletion into three different wild-type strains, M5, SP1 and W303-1A. This set of strains will aid further studies on the molecular basis of the complex pleiotropic phenotypes of ggs1/tps1 mutants. The phenotypes conferred by specific alleles were clearly dependent on the genetic background and also differed for some of the alleles. Our results show that the lethality caused by single gene deletion in one genetic background can become undetectable in another background. The sporulation defect of ggs1/tps1 diploids was neither due to a deficiency in G1 arrest, nor to the inability to accumulate trehalose. Ggs1/tps1 Δ mutants were very sensitive to glucose and fructose, even in the presence of a 100-fold higher galactose concentration. Fifty-percent inhibition occurred at concentrations similar to the Km values of glucose and fructose transport. The inhibitory effect of glucose in the presence of a large excess of galactose argues against an overactive glycolytic flux as the cause of the growth defect. Deletion of genes of the glucose carrier family shifted the 50% growth inhibition to higher sugar concentrations. This finding allows for a novel approach to estimate the relevance of the many putative glucose carrier genes in S. cerevisiae. We also show that the GGS1/TPS1 gene product is not only required for the transition from respirative to fermentative metabolism but continuously during logarithmic growth on glucose, in spite of the absence of trehalose under such conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00313424
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  • 3
    Electronic Resource
    Electronic Resource
    The nucleotide sequence of a 2·1 kb fragment from chromosome VI of Saccharomyces cerevisiae identifies a tRNAGly gene, part of a delta element and a palindromic sequence (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1107-1110 
    Details
    ISSN: 0749-503X
    Keywords: Yeast ; Saccharomyces cerevisiae ; chromosome VI ; tRNAGly ; delta element ; diacylglycerol kinase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The nucleotide sequence was determined of a 2·1 kb DNA fragment located at approximately 35 kb to the right of the centromere of chromosome VI from Saccharomyces cerevisiae. Analysis revealed the presence of a tRNAGLy gene, part of a delta element and a remarkable palindromic sequence. The longest open reading frame found encodes a putative protein of 195 amino acids. Although the fragment was isolated by hybridization to a human diacylglycerol kinase cDNA, no evidence was obtained for the presence of a gene encoding diacylglycerol kinase.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091011
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