Molecular and General Genetics MGG

, Volume 156, Issue 1, pp 99–105

A partial defect in carbon catabolite repression in mutants of Saccharomyces cerevisiae with reduced hexose phosphyorylation


  • K. -D. Entian
    • Institut für MikrobiologieTechnische Hochschule Darmstadt
  • F. K. Zimmermann
    • Institut für MikrobiologieTechnische Hochschule Darmstadt
  • I. Scheel
    • Institut für MikrobiologieTechnische Hochschule Darmstadt

DOI: 10.1007/BF00272258

Cite this article as:
Entian, K.-., Zimmermann, F.K. & Scheel, I. Molec. Gen. Genet. (1977) 156: 99. doi:10.1007/BF00272258


Mutants of Saccharomyces cerevisiae with reduced glucose phosphorylation were investigated. They were all recessive and belonged to one gene HEX1, mutant designation hex1. Carbon catabolite repression of alpha-glucosidases, invertase and part of the total malate dehydrogenase was reduced. Repression of the glyoxylate cycle enzymes, isocitrate lyase and malate synthetase, as well as that of gluconeogenetic fructose-1, 6-bisphosphatase was normal. A slight effect on repression of succinate: cytochrome c oxidoreductase and respiration was to be detected. The effect on repression by fructose was much less pronounced but still clear. However, there was a paradoxical effect of hexose concentration with higher concentrations repressing less. Maltose was also less repressing in the mutant. Growth on all sugars degraded via the hexose phosphorylation reaction was reduced and more strongly so at higher concentrations. Intracellular concentrations of glucose-6-phosphate, fructose-6-phosphate and fructose-1,6-bisphosphate were largely the same in mutant and wild type. The only striking difference between mutant and wild type was a fourfold higher intracellular glucose concentration in maltose grown mutants cells. The data obtained do not support the contention that carbon catabolite repression of the enzymes studied is triggered by intracellular hexoses or their metabolites alone. They rather suggest that it is some component of the hexose phosphorylating system that contributes to carbon catabolite repression.

Download to read the full article text

Copyright information

© Springer-Verlag 1977