Genetics of the Synthesis of serine from glycine and the utilization of glycine as sole nitrogen source by Saccharomyces cerevisiae

Saccharomyces cerevisiae can grow on glycine as sole nitrogen source and can convert glycine to serine via the reaction catalyzed by the glycine decarboxylase multienzyme complex (GDC). Yeast strains with mutations in the single gene for lipoamide dehydrogenase (lpd1) lack GDC activity, as well as t...

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Published inGenetics (Austin) Vol. 140; no. 4; pp. 1213 - 1222
Main Authors Sinclair, D.A. (The University of New South Wales, NSW, Australia.), Dawes, I.W
Format Journal Article
LanguageEnglish
Published United States Genetics Soc America 01.08.1995
Genetics Society of America
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Summary:Saccharomyces cerevisiae can grow on glycine as sole nitrogen source and can convert glycine to serine via the reaction catalyzed by the glycine decarboxylase multienzyme complex (GDC). Yeast strains with mutations in the single gene for lipoamide dehydrogenase (lpd1) lack GDC activity, as well as the other three 2-oxoacid dehydrogenases dependent on this enzyme. The LPD1 gene product is also required for cells to utilize glycine as sole nitrogen source. The effect of mutations in LPD1 (L-subunit of GDC), SER1 (synthesis of serine from 3-phosphoglycerate), ADE3 (cytoplasmic synthesis of one-carbon units for the serine synthesis from glycine), and all combinations of each has been determined. The results were used to devise methods for isolating mutants affected either in the generation of one-carbon units from glycine (via GDC) or subsequent steps in serine biosynthesis. The mutants fell into six complementation groups (gsd 1-6 for defects in conversion of glycine to serine). Representatives from three complementation groups were also unable to grow on glycine as sole nitrogen source (gsd l-3). Assays of the rate of glycine uptake and decarboxylation have provided insights into the nature of the mutations
Bibliography:9612716
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ISSN:0016-6731
1943-2631
1943-2631
DOI:10.1093/genetics/140.4.1213