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Abelson-transformed fibroblasts contain nuclear phosphotyrosyl-proteins which preferentially bind to murine DNA

J C Bell, L C Mahadevan, W H Colledge

    Nature
    |February 5, 1987
    PubMed

    Insights

    Protein-tyrosine kinases regulate cell growth. This study identifies nuclear phosphotyrosyl-proteins in transformed cells that bind DNA, suggesting a mechanism for kinase-mediated gene transcription changes.

    Area of Science:

    • Molecular Biology
    • Cell Biology
    • Biochemistry

    Background:

    • Protein-tyrosine kinases are crucial regulators of cell growth and transformation, often acting as growth-factor receptors or oncogene products.
    • A key question is how kinase substrates influence gene expression changes, impacting cellular processes.
    • DNA-binding proteins offer a direct mechanism for regulating gene transcription.

    Purpose of the Study:

    • To investigate if DNA-binding proteins can be substrates of protein-tyrosine kinases.
    • To identify nuclear phosphotyrosyl-proteins in v-abl-transformed murine fibroblasts.
    • To determine if these proteins exhibit selective DNA-binding properties.

    Main Methods:

    • Affinity competition chromatography using bacterial and mouse DNA.
    • Analysis of nuclear phosphotyrosyl-proteins in normal and v-abl-transformed murine fibroblasts.
    • Phosphorylation assays to detect protein-tyrosine kinase activity.

    Main Results:

    • Evidence of nuclear phosphotyrosyl-proteins in v-abl-transformed murine fibroblasts.
    • These proteins were found to be significantly less phosphorylated in normal NIH 3T3 cells.
    • Some identified phosphotyrosyl-proteins demonstrated preferential binding to mouse DNA.

    Conclusions:

    • Nuclear phosphotyrosyl-proteins exist in v-abl-transformed cells.
    • These proteins possess DNA-binding capabilities, with some showing species selectivity.
    • This suggests a novel pathway where protein-tyrosine kinases modulate gene transcription via specific DNA-binding protein substrates.

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