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Processiveness of DNA polymerases. A comparative study using a simple procedure.

S K Das, R K Fujimura

    The Journal of Biological Chemistry
    |February 25, 1979
    PubMed
    Summary
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    We developed a method to measure DNA polymerase processiveness, finding most enzymes are "quasi-processive" adding 10-15 nucleotides. T5 DNA polymerase, however, is highly processive, replicating templates extensively.

    Area of Science:

    • Molecular Biology
    • Enzymology
    • Biochemistry

    Background:

    • DNA polymerases are crucial enzymes for DNA replication and repair.
    • Understanding DNA polymerase processiveness is key to elucidating DNA synthesis mechanisms.

    Purpose of the Study:

    • To develop a simple and generalizable method for analyzing DNA polymerase processiveness.
    • To quantify the processiveness of various DNA polymerases, including Escherichia coli DNA polymerase I, T4 DNA polymerase, and calf thymus alpha- and beta-DNA polymerases.

    Main Methods:

    • A novel assay was designed using poly(dA)300:oligo(dT)10 primer-template under conditions limiting enzyme re-utilization.
    • Product isolation via oligo(dT)-cellulose chromatography.
    • Quantification of incorporated nucleotides using radiolabeled precursors and enzymatic digestion.

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    Main Results:

    • Most tested DNA polymerases (E. coli DNA polymerase I, T4, calf thymus alpha/beta) exhibited "quasi-processive" behavior, adding ~10-15 nucleotides per binding event.
    • T5 DNA polymerase demonstrated high processiveness, replicating templates until near the 5' end.
    • Nicked DNA templates increased E. coli DNA polymerase I processiveness 2-2.5 fold.

    Conclusions:

    • The developed method provides a reliable way to assess DNA polymerase processiveness.
    • Enzyme processiveness varies significantly, impacting DNA replication and repair dynamics.
    • Increased processiveness on nicked DNA suggests implications for DNA repair patch size determination.