Hypoxanthine: guanine phosphoribosyltransferase mutants in Saccharomyces cerevisiae.

Hypoxanthine: guanine phosphoribosyltransferase mutants in Saccharomyces cerevisiae.
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次黄嘌呤:酿酒酵母中的鸟嘌呤磷酸核糖基转移酶突变体。

DOI:
10.1007/bf00425755
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发表时间:
1983
期刊:
Molecular & general genetics : MGG
影响因子:
--
通讯作者:
Filpula,D
Filpula,D
中科院分区:
--
文献类型:
--
作者:
Woods,RA;Roberts,DG;Friedman,T;Jolly,D;Filpula,D

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Yeast mutants lacking activity of the enzyme hypoxanthine: guanine phosphoribosyltransferase (H:GPRT) have been isolated by selecting for resistance to 8-azaguanine in a strain carrying the wild type allele,ade4+of the gene coding for amidophosphoribosyltransferase (PRPPAT), the first enzyme ofde novopurine synthesis. The mutants excrete purines and are cross-resistant to 8-azaadenine. They are recessive and represent a single complementation group, designatedhpt1. Ade4-su, a prototrophic allele ofade4with reduced activity of PRPPAT, is epistatic tohpt1, suppressing purine excretion and resistance to azaadenine but not resistance to azaguanine. The genotypeade2 hpt1does not respond to hypoxanthine.Hpt1complements and is not closely linked to the purine excreting mutantspur1topur5. Hpt1andpur6, a regulatory mutant of PRPPAT, are also unlinked but do not complement, suggesting a protein-protein interaction between H:G-PRT and PRPPAT. Mycophenolic acid (MPA), an inhibitor ofde novoguanine nucleotide synthesis, inhibits the growth ofhpt1andhpt1+. Xanthine allows both genotypes to grow in the presence of MPA whereas guanine only allows growth ofhpt1+. Activity of A-PRT, X-PRT and H:G-PRT is present inhpt+.Hpt1lacks activity of H:G-PRT but has normal A-PRT and X-PRT.
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