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DNA polymerases from bakers' yeast.

L M Chang

    The Journal of Biological Chemistry
    |March 25, 1977
    PubMed
    Summary
    This summary is machine-generated.

    Researchers identified two distinct DNA polymerases in baker's yeast: Yeast DNA polymerase I and Yeast DNA polymerase II. These enzymes exhibit unique properties and are not identical to known polymerases, suggesting novel roles in yeast DNA replication.

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    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Yeast Genetics

    Background:

    • Saccharomyces cerevisiae (baker's yeast) is a model organism for studying eukaryotic cellular processes.
    • DNA polymerases are essential enzymes responsible for DNA replication, repair, and recombination.
    • Understanding the diversity and properties of DNA polymerases is crucial for deciphering DNA metabolism.

    Purpose of the Study:

    • To identify and characterize DNA polymerases in commercial baker's yeast (Saccharomyces cerevisiae).
    • To differentiate between distinct yeast DNA polymerase species based on biochemical and immunological properties.
    • To compare yeast DNA polymerases with known eukaryotic and prokaryotic DNA polymerases.

    Main Methods:

    • Enzyme purification using DEAE-cellulose, hydroxylapatite, and denatured DNA-cellulose chromatography.

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  • Immunological cross-reactivity analysis to distinguish enzyme species.
  • Assay of associated enzyme activities, including nuclease activity, pyrophosphate exchange, pyrophosphorolysis, and deoxynucleoside triphosphate degradation.
  • Assessment of template utilization and mismatched nucleotide excision.

    • Main Results:

    • Two distinct high-molecular-weight DNA polymerases, Yeast DNA polymerase I and Yeast DNA polymerase II, were purified.
    • The two enzymes lacked immunological cross-reactivity, confirming they are separate species.
    • Enzyme I exhibited 3'-exonuclease activity but no deoxynucleoside triphosphate degradation, while Enzyme II showed template-dependent deoxynucleoside triphosphate degradation and mismatched nucleotide excision.
    • Both enzymes were inhibited by N-ethylmaleimide.

    Conclusions:

    • Yeast DNA polymerase I shares similarities with eukaryotic DNA polymerase alpha.
    • Yeast DNA polymerase II exhibits properties analogous to prokaryotic DNA polymerases II and III.
    • These yeast DNA polymerases are distinct from previously identified eukaryotic and prokaryotic DNA polymerases.