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DNA polymerase alpha cofactors C1C2 function as primer recognition proteins.

C G Pritchard, D T Weaver, E F Baril

    The Journal of Biological Chemistry
    |August 25, 1983
    PubMed
    Summary
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    Two proteins, C1 and C2, significantly enhance DNA polymerase alpha activity by acting as primer recognition proteins. They facilitate DNA synthesis initiation by preventing nonproductive binding to single-stranded DNA, enabling efficient primer recognition.

    Area of Science:

    • Molecular Biology
    • Enzymology

    Background:

    • DNA polymerase alpha is crucial for DNA replication.
    • Its activity is regulated by accessory proteins.
    • Understanding these interactions is key to comprehending DNA synthesis.

    Purpose of the Study:

    • To investigate the role of two associated proteins, C1 and C2, in regulating DNA polymerase alpha activity.
    • To determine the mechanism by which C1 and C2 modulate enzyme function.
    • To elucidate the primer recognition capabilities of the C1C2 complex.

    Main Methods:

    • Complexation analysis of DNA polymerase alpha with C1 and C2 in human and monkey cells.
    • Enzyme activity assays using various DNA and RNA-primed DNA templates.
    • Reconstitution experiments with purified alpha polymerase and C1C2 complex.

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  • Kinetic analysis (Km values) and processivity studies.

    • Main Results:

    • Most DNA polymerase alpha exists in a complex with C1 and C2, which stimulates activity 180-1800 fold on specific primer-template substrates.
    • C1C2 specifically enhances alpha polymerase from the same cell type.
    • C1C2 decreases Km for DNA and primer, increases use of shorter primers, and stimulates initial nucleotide incorporation.
    • C1C2 does not affect Km for deoxynucleotides, sequence-specific arrest, or processivity.

    Conclusions:

    • C1C2 proteins function as primer recognition proteins for DNA polymerase alpha.
    • They enhance DNA synthesis initiation by preventing nonproductive binding to single-stranded DNA.
    • This allows the enzyme to efficiently locate and bind to primers for DNA replication.