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  • 11
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 11 (1995), S. 137-144 
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; HXK1 ; HXK2 ; GLK1 ; mRNA ; transcriptional control ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In Saccharomyces cerevisiae, the transcriptional regulation of most glycolytic genes has been extensively studied. By contrast, little is known about the transcriptional control of the three glucose-phosphorylating enzymes, although this catalytic reaction has an important role in the regulation of cell metabolism. In this paper, we describe the transcriptional regulation of the HXK1, HXK2 and GLK1 genes in the hope of revealing differences in the steady-state levels of mRNA associated with a particular carbon source used in the culture medium. Our results provide evidence supporting a differential expression of the three genes depending on the carbon source used for growth. We have also studied the induction and repression kinetics of mRNA expression for the HXK1, HXK2 and GLK1 genes.
    Additional Material: 4 Ill.
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  • 12
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 11 (1995), S. 1393-1398 
    ISSN: 0749-503X
    Keywords: glucose transport ; hexose diffusion ; sugar transport ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: It has been claimed that the low-affinity component of glucose transport in Saccharomyces cerevisiae is due to passive diffusion of the sugar across the plasma membrane. We have investigated this possibility. For this purpose we have measured the permeability coefficient of hexoses in this organism. We have found that this coefficient is at least two to three orders of magnitude lower than required to account for the low-affinity component of glucose transport, and have concluded that this component is not due to passive diffusion.
    Additional Material: 2 Ill.
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  • 13
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 2 (1986), S. 101-108 
    ISSN: 0749-503X
    Keywords: L-Arabinose ; D-xylose ; UDP-glucose 4-epimerase ; inactivation ; Saccharomyces ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In a previous paper (Cármenes et al., 1984) we reported that UDP-glucose 4-epimerase from Saccharomyces was inactivated both in vitro (Crude extracts) by L-arabinose or D-xylose. In this paper, we reported that pure epimerase requires the presence of UMP or UDP to be inactivated by sugars and that the inactivation is due to the reduction of the epimerase NAD+, which is essential for epimerase activity. The inactivation rate is directly proportional to epimerase and sugar concentrations and hyperbolically proportional to UMP concentration. In situ experiments made with permeabilized cells showed that epimerase is inactivated in the same way when it is inside the cell. In vivo studies showed that epimerase is inactivated to a smaller extent when 1% Dgalactose is present in the culture medium than when 1% ethanol is the main carbon source.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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