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. 1983 Jan;153(1):574–578. doi: 10.1128/jb.153.1.574-578.1983

Pleiotropic mutations regulating resistance to glucose repression in Saccharomyces carlsbergensis are allelic to the structural gene for hexokinase B.

C A Michels, K M Hahnenberger, Y Sylvestre
PMCID: PMC217414  PMID: 6848488

Abstract

Previously, we described a mutation glr1-1 in Saccharomyces carlsbergensis which pleiotropically relieves the synthesis of the following enzymes from glucose repression: maltase, galactokinase, alpha-galactosidase, NADH:cytochrome c reductase, and cytochrome c oxidase (C. A. Michels and A. Romanowski, J. Bacteriol, 143:674-679, 1980.) In this report, we demonstrate that glr1-1 and two other alleles, glr1-3 and glr1-16, are also insensitive to the glucose repression of invertase synthesis. Determinations of the levels of hexokinase activity and the rate of glucose transport in these mutants show that both are reduced as compared with the parent strain. Complementation tests and genetic analysis indicate that the glr1 mutations are allelic to HXK2, the structural gene for hexokinase B. The significance of this result is discussed with regard to the mechanism of glucose repression in S. carlsbergensis.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Adams B. G. Induction of galactokinase in Saccharomyces cerevisiae: kinetics of induction and glucose effects. J Bacteriol. 1972 Aug;111(2):308–315. doi: 10.1128/jb.111.2.308-315.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. CIRILLO V. P. Mechanism of glucose transport across the yeast cell membrane. J Bacteriol. 1962 Sep;84:485–491. doi: 10.1128/jb.84.3.485-491.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Carlson M., Botstein D. Two differentially regulated mRNAs with different 5' ends encode secreted with intracellular forms of yeast invertase. Cell. 1982 Jan;28(1):145–154. doi: 10.1016/0092-8674(82)90384-1. [DOI] [PubMed] [Google Scholar]
  4. Chapman C., Bartley W. The kinetics of enzyme changes in yeast under conditions that cause the loss of mitochondria. Biochem J. 1968 Apr;107(4):455–465. doi: 10.1042/bj1070455. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Entian K. D. A carbon catabolite repression mutant of Saccharomyces cerevisiae with elevated hexokinase activity: evidence for regulatory control of hexokinase PII synthesis. Mol Gen Genet. 1981;184(2):278–282. doi: 10.1007/BF00272917. [DOI] [PubMed] [Google Scholar]
  6. Entian K. D. Genetic and biochemical evidence for hexokinase PII as a key enzyme involved in carbon catabolite repression in yeast. Mol Gen Genet. 1980;178(3):633–637. doi: 10.1007/BF00337871. [DOI] [PubMed] [Google Scholar]
  7. Entian K. D., Mecke D. Genetic evidence for a role of hexokinase isozyme PII in carbon catabolite repression in Saccharomyces cerevisiae. J Biol Chem. 1982 Jan 25;257(2):870–874. [PubMed] [Google Scholar]
  8. Entian K. D., Zimmermann F. K. Glycolytic enzymes and intermediates in carbon catabolite repression mutants of Saccharomyces cerevisiae. Mol Gen Genet. 1980 Jan;177(2):345–350. doi: 10.1007/BF00267449. [DOI] [PubMed] [Google Scholar]
  9. Entian K. D., Zimmermann F. K., Scheel I. A partial defect in carbon catabolite repression in mutants of Saccharomyces cerevisiae with reduced hexose phosphyorylation. Mol Gen Genet. 1977 Nov 4;156(1):99–105. doi: 10.1007/BF00272258. [DOI] [PubMed] [Google Scholar]
  10. Gancedo J. M., Clifton D., Fraenkel D. G. Yeast hexokinase mutants. J Biol Chem. 1977 Jul 10;252(13):4443–4444. [PubMed] [Google Scholar]
  11. Kew O. M., Douglas H. C. Genetic co-regulation of galactose and melibiose utilization in Saccharomyces. J Bacteriol. 1976 Jan;125(1):33–41. doi: 10.1128/jb.125.1.33-41.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lobo Z., Maitra P. K. Genetics of yeast hexokinase. Genetics. 1977 Aug;86(4):727–744. doi: 10.1093/genetics/86.4.727. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Maitra P. K., Lobo Z. A kinetic study of glycolytic enzyme synthesis in yeast. J Biol Chem. 1971 Jan 25;246(2):475–488. [PubMed] [Google Scholar]
  14. Matsumoto K., Uno I., Oshima Y., Ishikawa T. Isolation and characterization of yeast mutants deficient in adenylate cyclase and cAMP-dependent protein kinase. Proc Natl Acad Sci U S A. 1982 Apr;79(7):2355–2359. doi: 10.1073/pnas.79.7.2355. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Matsumoto K., Uno I., Toh-E A., Ishikawa T., Oshima Y. Cyclic AMP may not be involved in catabolite repression in Saccharomyes cerevisiae: evidence from mutants capable of utilizing it as an adenine source. J Bacteriol. 1982 Apr;150(1):277–285. doi: 10.1128/jb.150.1.277-285.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Michels C. A., Romanowski A. Pleiotropic glucose repression-resistant mutation in Saccharomyces carlesbergensis. J Bacteriol. 1980 Aug;143(2):674–679. doi: 10.1128/jb.143.2.674-679.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Perlman P. S., Mahler H. R. Derepression of mitochondria and their enzymes in yeast: regulatory aspects. Arch Biochem Biophys. 1974 May;162(1):248–271. doi: 10.1016/0003-9861(74)90125-8. [DOI] [PubMed] [Google Scholar]
  18. Polakis E. S., Bartley W. Changes in the enzyme activities of Saccharomyces cerevisiae during aerobic growth on different carbon sources. Biochem J. 1965 Oct;97(1):284–297. doi: 10.1042/bj0970284. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Van Wijk R., Ouwehand J., van den Bos T., Koningsberger V. V. Induction and catabolite repression of alpha-glucosidase synthesis in protoplasts of Saccharomyces carlsbergensis. Biochim Biophys Acta. 1969 Jul 22;186(1):178–191. doi: 10.1016/0005-2787(69)90501-2. [DOI] [PubMed] [Google Scholar]
  20. Zimmermann F. K., Scheel I. Mutants of Saccharomyces cerevisiae resistant to carbon catabolite repression. Mol Gen Genet. 1977 Jul 7;154(1):75–82. doi: 10.1007/BF00265579. [DOI] [PubMed] [Google Scholar]
  21. van Rijn J., van Wijk R. Differential sensitivities of the two malate dehydrogenases and the maltose permease to the effect of glucose in Saccharomyces carlsbergensis. J Bacteriol. 1972 May;110(2):477–484. doi: 10.1128/jb.110.2.477-484.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. van de Poll K. W., Kerkenaar A., Schamhart D. H. Isolation of a regulatory mutant of fructose-1,6-diphosphatase in Saccharomyces carlsbergensis. J Bacteriol. 1974 Mar;117(3):965–970. doi: 10.1128/jb.117.3.965-970.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]

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