The ADE2 gene of Saccharomyces cerevisiae yeast encodes aminoimidazole ribonucleotide-carboxylase (AIR-carboxylase), an enzyme catalyzing the sixth stage of purine nucleotide biosynthesis. Strains bearing the ade2 mutation are able to grow on a glucose-containing synthetic medium with the addition of adenine or hypoxanthine, which under the action of the cellular phosphoribosyltransferases are converted into adenosine monophosphate and inosine monophosphate, respectively. Our studies showed that ade2 mutants were unable to grow on a synthetic medium with glycerol and hypoxanthine. This newly described feature is not constitutively manifested, because some strains can contain suppressor mutations which restore the ability to grow on a synthetic medium with glycerol and hypoxanthine. The ade4, ade5, ade8, ade6, and ade7 mutations were found to suppress the phenotypic manifestation of the ade2 mutations via inactivation of enzymes catalyzing the first, second, third, fourth and fifth stages of purine biosynthesis, while the ade1 mutation, which inactivates enzyme of the seventh stage, lacks suppressive activity. Strains with single adenine mutations, ade4, ade5, ade8, ade6, ade7, or ade1 grow on glycerol- and hypoxanthine-containing media. Our data suggest that the new property of the ade2 mutations could be associated with the accumulation of the AIR-carbole-ribonucleotide. A mutation resulting in the requirement for serine on the medium with glycerol, but not glucose, is described.
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|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
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