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Focus Formation: A Cell-based Assay to Determine the Oncogenic Potential of a Gene
08:18

Focus Formation: A Cell-based Assay to Determine the Oncogenic Potential of a Gene

Published on: December 31, 2014

Interaction of the oncogene protein myc with specific DNA fragments

K Moelling, T Sander, U Lorenz

    Journal of Cancer Research and Clinical Oncology
    |January 1, 1986
    PubMed

    Insights

    The p110gag-myc protein binds preferentially to cellular DNA flanking the MC29 retrovirus integration site. This finding refutes the autoregulatory model of viral gene expression.

    Area of Science:

    • Molecular Biology
    • Retroviral Research
    • Protein-DNA Interactions

    Background:

    • The MC29 retrovirus encodes the p110gag-myc protein, a potential regulator of viral gene expression.
    • Previous hypotheses suggested an autoregulatory model where the protein binds to the viral LTR promoter/enhancer region.

    Purpose of the Study:

    • To investigate the DNA-binding properties of the purified p110gag-myc protein.
    • To determine if the protein interacts with viral or cellular DNA sequences.

    Main Methods:

    • Purification of p110gag-myc protein using immuno-affinity chromatography.
    • Filter binding assays to study protein-DNA interactions with fragments from a MC29 DNA clone.
    • Agarose gel electrophoresis to analyze DNA fragments retained by the protein.

    Main Results:

    • The p110gag-myc protein was purified 3,000-fold.
    • Preferential binding of the protein to a DNA fragment from flanking cellular sequences was observed.
    • No preferential binding to the viral LTR promoter/enhancer region was detected.

    Conclusions:

    • The p110gag-myc protein interacts with flanking cellular DNA, not the viral LTR.
    • The autoregulatory model for MC29 retrovirus gene expression is not substantiated by these findings.

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