Summary
Two unlinked loci controlling the glucose-repressible alcohol dehydrogenase (ADH II) inSaccharomyces cerevisiae were investigated. One locus (AD R2) was characterized by electrophoreticallyslow andfast alleles and by inactiveadr2 mutant alleles. The ADH II pattern of heteroallelicslow × fast diploids indicates a tetrameric structure of the enzyme.AD R2 was considered as the structural gene, which codes for the ADH II subunits. Allelicadr2-f mutants could be classified by their response to theslow wild type allele (AD R2-S) in heter ozyg ous diploids. In most cases, only the slow band appeared. In threeadr2-f/AD R2-S crosses hybrid enzymes between inactive fast and active slow enzymes were formed. It was demonstrated, that allelic interactions at the protein level are not restricted to electrophoretical behaviour of hybrid enzymes. They also influence specific activities and substrate affinities.
The other locus investigated,AD R1, was characterized by ADH II negative mutants (adr1) and by allelic mutants which generate only very low activity (AD R1-L).ADR1 does not influence the electrophoretic properties of slow and fast ADH II proteins.adr1 mutants have an intact structural gene, which is not expressed. The gene has probably a regulatory function with respect to ADH II synthesis.
Similar content being viewed by others
References
Bergmeyer, H. U., Bernt, E.: Alkoholdehydrogenase. In: Methoden der enzymatischen Analyse. 2. Aufl., Bd. 1. Weinheim/Bergstr.: Verlag Chemie 1970
Ciriacy, M.: Genetics of alcohol dehydrogense inSaccharomyces cerevisiae. I. Isolation and genetic analysis of adh mutants. Mutat. Res. (In press) (1975)
Fincham, J. R. S.: Genetic complementation. New York: Benjamin 1966
Harris, J. I.: The structure and catalytic activity of thiol dehydrogenases. In: Structure and activities of enzymes, pp. 97–109. (ed. by Goodwin, T. W.et al.) New York: Academic Press 1964
Lowry, O. H., Rosebrough, N. J., Farr, A. L., Randall, R. J.: Protein measurement with the Folin phenol reagent. J. biol. Chem.193, 265–275 (1951)
Lutstorf, U., Megnet, R.: Multiple forms of alcohol dehydrogenase inSaccharomyces cerevisiae. I. Physiological control of ADH-2 and properties of ADH-2 and ADH4. Arch. Biophys. Biochem,126, 933–944 (1968)
Markert, C.: The molecular basis for isozymes. Ann. N. Y. Acad. Sci.151, 14–40 (1968)
Poulik, M. D.: Starch gel electrophoresis in a discontinuous system of buffers. Nature (Lond.)180, 1477 (1957)
Roman, H.: A system selective for mutations affecting the synthesis of adenine in yeast. R. Lab. Carlsberg, Ser. Physiol.26, 299–314 (1956)
Scandalios, J. G.: Genetic control of multiple molecular forms of enzymes in plants: a review. Biochem. Genet.3, 37–79 (1969)
Shaw, C. R.: Electrophoretic variation in enzymes. Science149, 936–943 (1965)
Shaw, C. R.: Isozymes: Classification, frequency and significance. Int. Rev. Cytol.25, 297–332 (1969)
Yu, S. A., Gasset, M. K., Sussman, A. S.: Genetic control of multiple forms of trehalase inNeurospora crassa. Genetics68, 473–481 (1971)
Zimmermann, F. K., Schmiedt, I., Berge, A. M. A. ten: Dominance and recessivness at the protein level in mutant x wildtype crosses inSaccharomyces cerevisiae. Molec. gen. Genet.104, 321–330 (1969)
Author information
Authors and Affiliations
Additional information
Communicated by H. Böhme
Rights and permissions
About this article
Cite this article
Ciriacy, M. Genetics of alcohol dehydrogenase inSaccharomyces cerevisiac . Molec. Gen. Genet. 138, 157–164 (1975). https://doi.org/10.1007/BF02428119
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF02428119