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Functional mutants of yeast alcohol dehydrogenase affecting kinetics, cellular redox balance, and electrophoretic mobility

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Abstract

Repeated selection of petite (respiratorily incompetent) Saccharomyces cerevisiae on medium containing allyl alcohol, both on plates and in the turbidostat, results in mutants with a remarkably similar response. Most of the mutations affect the constitutive alcohol dehydrogenase, resulting in enzymes with a cathodal shift in electrophoretic mobility, and none shows a significant anodal shift. The genetics, kinetics, and physiological effect of three of the mutants have been investigated in detail, and while all confer resistance to allyl alcohol through a shift in the NAD/NADH ratio, they do so in slightly different ways. The potential of this system for exploring the range of short-term adaptations open to this organism is discussed.

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This work was supported by Grant GM 19967 from the National Institutes of Health, U.S. Public Health Service.

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Wills, C., Phelps, J. Functional mutants of yeast alcohol dehydrogenase affecting kinetics, cellular redox balance, and electrophoretic mobility. Biochem Genet 16, 415–432 (1978). https://doi.org/10.1007/BF00484208

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  • DOI: https://doi.org/10.1007/BF00484208

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