Catabolite inactivation of the glucose transport system in Saccharomyces cerevisiae.
The sugar transport systems of Saccharomyces cerevisiae are irreversibly inactivated when protein synthesis is inhibited. This inactivation is responsible for the drastic decrease in fermentation observed in ammonium-starved yeast and is related to the occurrence of the Pasteur effect in these cells. Our study of the inactivation of the glucose transport system indicates that both the high-affinity and the low-affinity components of this system are inactivated. Inactivation of the high-affinity component evidently requires the utilization of a fermentable substrate by the cells, since inactivation did not occur during carbon starvation, when a fermentable sugar was added to starved cells, inactivation began, when the fermentation inhibitors iodoacetate or arsenate were added in addition to sugars, the inactivation was prevented, when a non-fermentable substrate was added instead of sugars, inactivation was also prevented. The inactivation of the low-affinity component appeared to show similar requirements. It is concluded that the glucose transport system in S. cerevisiae is regulated by a catabolite-inactivation process.
D000255:Adenosine Triphosphate / Q000378:metabolism; D001692:Biological Transport; D002268:Carboxypeptidases / Q000378:metabolism; D043402:Cathepsin A; D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000378:metabolism; D000431:Ethanol / Q000378:metabolism; D005947:Glucose / Q000378:metabolism*; D007700:Kinetics; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins; D014994:Xylose / Q000378:metabolism
D029701:Saccharomyces cerevisiae Proteins; D000431:Ethanol; D000255:Adenosine Triphosphate; D014994:Xylose; D002268:Carboxypeptidases; D010450:Endopeptidases; D043402:Cathepsin A; C499283:PRC1 protein, S cerevisiae; C022633:serine carboxypeptidase; C019836:CPS1 protein, S cerevisiae; D003546:Cysteine Endopeptidases; C028307:endopeptidase B; D005947:Glucose