Adenine phosphoribosyltransferase mutants in Saccharomyces cerevisiae

• Published in: Journal of general microbiology Vol. 130; no. 10; pp. 2629 - 2637
• Main Authors: Woods, R.A, Roberts, D.G, Stein, D.S, Filpula, D
• Format: Journal Article
• Language: English
• Published: London Soc General Microbiol 01-10-1984; New York, NY Cambridge University Press
• Subjects: Adenine Phosphoribosyltransferase - metabolism; Alleles; Amidophosphoribosyltransferase - genetics; Aminohydrolases - metabolism; Biological and medical sciences; Electrophoresis; Fundamental and applied biological sciences. Psychology; Genotype; Growth, nutrition, metabolism, transports, enzymes. Molecular biology; Hypoxanthine Phosphoribosyltransferase - metabolism; Microbiology; mutants; Mutation; Mycology; Pentosyltransferases - metabolism; Saccharomyces cerevisiae; Saccharomyces cerevisiae - enzymology; Saccharomyces cerevisiae - genetics; transferases; Yeast; Enzyme; Characterization; Fungi; Enzymatic activity; Electrophoresis; Isolation; Purine; Amidophosphoribosyltransferase; Mutation; Adenine phosphoribosyltransferase; Saccharomyces cerevisiae; Thallophyta
• ISSN: 0022-1287; 1350-0872; 1465-2080
• DOI: 10.1099/00221287-130-10-2629

1 Department of Biology, University of Winnipeg. Winnipeg, Manitoba, Canada R3B 2E9
1 Department of Pediatrics, University of California, San Diego, California 92093, USA
ABSTRACT
SUMMARY: Mutants of Saccharomyces cerevisiae deficient in adenine phosphoribosyltransferase (A-PRT, EC 2.4.2.7 ) have been isolated following selection for resistance to 8-azaadenine in a prototrophic strain carrying the ade4-su allele of the gene coding for amidophosphoribosyltransferase(EC 2.4.2.14 ). The mutants were recessive and defined a single gene, aptl. They did not excrete purine when combined with ade4 * . The mutants appeared to retain some A-PRT activity in crude extracts, and strains of the genotype ade2 aptl responded to both adenine and hypoxanthine. Mutants deficient in adenine aminohydrolase (EC 3.5.4.2 ) activity, aahl , and hypoxanthine: guanine phosphoribosyltransferase (EC 2.4.2.8 ) activity, hptl , were used to synthesize the genotypes aptl hptl aah * and aptl hpt* aahl. The absence of A-PRT activity in strains with these genotypes confirmed the hypothesis that the residual A-PRT activity of aptl mutants was due to adenine aminohydrolase and hypoxanthine:guanine phosphoribosyltransferase acting in concert.
Present address: Genex Corporation, Gaithersberg, Maryland, 20877, USA.
Present address: Department of Genetics, Stanford University, Stanford, California, USA.