Replacement of the promoter of the yeast plasma membrane ATPase gene by a galactose-dependent promoter and its physiological consequences.
In order to probe the physiological role of the yeast plasma membrane ATPase we have replaced the constitutive promoter of its gene by a galactose-dependent promoter. The resulting cells stop growing on glucose medium when the preformed ATPase is diluted to 20% of normal. There is a correlation between ATPase activity and both proton efflux from the cells and amino acid transport. A large proportion of growth-arrested cells appear enlarged and with several buds containing nuclei.
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Instituto de Investigaciones Biomédicas del CSIC, Facultad de Medicina, Universidad Autónoma, Madrid, Spain.
Perona
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Serrano
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D000251:Adenosine Triphosphatases / Q000235:genetics*; D002462:Cell Membrane / Q000201:enzymology; D005690:Galactose / Q000494:pharmacology*; D005796:Genes; D005800:Genes, Fungal; D007700:Kinetics; D011401:Promoter Regions, Genetic / Q000187:drug effects; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics* / Q000254:growth & development
D000251:Adenosine Triphosphatases; D005690:Galactose