1887

Abstract

Growth of on D-glucono-δ-lactone (δgl) was found to be associated with a specific coordinate induction of the synthesis of two enzymes of the oxidative pentose phosphate pathway – 6-phosphogluconate dehydrogenase and 6-phosphogluconolactonase – together with that of a third enzyme, gluconokinase. The mutation, responsible for an approximately 80% loss of 6-phosphogluconate dehydrogenase activity and the inability of the cells to grow on δgl, completely abolished the induction of all three enzymes, while the mutation affected this only partially. One class of revertants, selected for growth on δgl, was found to have recovered normal dehydrogenase activity and the ability to synthesize the three enzymes when induced by δgl. Another class of δgl-positive revertants possessed constitutively elevated levels of gluconokinase. In contrast, glucose-positive revertants of , with restored constitutive dehydrogenase activity, continued to remain deficient in induction of the three enzymes and also failed to grow on δgl. Induction of 6-phosphogluconate dehydrogenase activity was associated with increased transcription of the gene coding for the major isoenzyme; the transcript remained undetectable in the mutant. Induction of these specific enzymes thus appears to be essential for growth of on δgl.

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/content/journal/micro/10.1099/00221287-138-9-1865
1992-09-01
2021-04-21
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References

  1. Brodie A. F., Lipmann F. 1955; Identification of a gluconolactonase. Journal of Biological Chemistry 212:677–685
    [Google Scholar]
  2. Carlson M., Botstein D. 1982; Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase. Cell 28:145–154
    [Google Scholar]
  3. Cohen S. S. 1955; Gluconokinase. Methods in Enzymology 1:350–354
    [Google Scholar]
  4. Fraenkel D. G. 1982; Carbohydrate metabolism. In The Molecular Biology of the Yeast Saccharomyces Metabolism and Gene Expression pp. 1–37 Edited by Strathern J. N., Jones E. W., Broach J. R. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  5. Fraenkel D. G. 1986; Mutants in glucose metabolism. Annual Review of Biochemistry 55:317–337
    [Google Scholar]
  6. Gancedo C., Delgado M. A. 1984; Isolation and characterization of a mutant from Saccharomyces cerevisiae lacking fructose 1,6-bisphosphatase. European Journal of Biochemistry 139:65–655
    [Google Scholar]
  7. Lobo Z., Maitra P. K. 1977; Genetics of yeast hexokinase. Genetics 86:727–744
    [Google Scholar]
  8. Lobo Z., Maitra P. K. 1982; Pentose phosphate pathway mutants of yeast. Molecular and General Genetics 185:367–368
    [Google Scholar]
  9. Maitra P. K., Lobo Z. 1971; A kinetic study of glycolytic enzyme synthesis in yeast. Journal of Biological Chemistry 246:475–488
    [Google Scholar]
  10. Peterson G. L. 1983; Determination of total protein. Methods in Enzymology 91:95–119
    [Google Scholar]
  11. Sherman F., Fink G. R., Hicks J. B. 1974 Laboratory Course Manual for Methods in Yeast Genetics Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  12. Sherman F., Fink G. R., Hicks J. B. 1986 Laboratory Course Manual for Methods in Yeast Genetics Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
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