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Related Experiment Videos

mRNA levels for the fermentative alcohol dehydrogenase of Saccharomyces cerevisiae decrease upon growth on a

C L Denis, J Ferguson, E T Young

    The Journal of Biological Chemistry
    |January 25, 1983
    PubMed
    Summary

    Alcohol dehydrogenase I in Saccharomyces cerevisiae is not constitutive. Its synthesis is repressed when yeast grow on non-fermentative carbon sources, indicating transcriptional regulation.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Yeast Genetics

    Background:

    • Alcohol dehydrogenase I (ADH I) in Saccharomyces cerevisiae was previously considered a constitutive enzyme.
    • Understanding the regulation of ADH I is crucial for comprehending yeast metabolism and adaptation.

    Purpose of the Study:

    • To investigate the regulation of alcohol dehydrogenase I synthesis in Saccharomyces cerevisiae.
    • To determine if ADH I is repressed by non-fermentative carbon sources and elucidate the underlying mechanism.

    Main Methods:

    • Yeast strains of Saccharomyces cerevisiae were grown on glucose and ethanol-containing media.
    • Protein synthesis rates were measured using radiolabeling.
    • mRNA levels were assessed through hybridization to the cloned ADCl gene.

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    Main Results:

    • Alcohol dehydrogenase I protein synthesis decreased significantly (6-10 fold) when yeast were shifted from glucose to ethanol or when glucose was depleted.
    • This decrease was correlated with a reduction in functional alcohol dehydrogenase I mRNA levels.
    • No significant increase in protein degradation was observed, and total mRNA levels mirrored functional mRNA levels.

    Conclusions:

    • Alcohol dehydrogenase I protein synthesis is repressed by growth on non-fermentative carbon sources.
    • Regulation occurs at the transcriptional level, affecting the amount of functional alcohol dehydrogenase I mRNA.
    • The enzyme is not constitutive as previously thought, but rather dynamically regulated.