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DNA-binding activity is associated with purified myb proteins from AMV and E26 viruses and is temperature-sensitive

K Moelling, E Pfaff, H Beug

    Cell
    |April 1, 1985
    PubMed

    Insights

    Avian myeloblastosis virus (AMV) and avian leukemia virus E26 (E26) oncogene proteins bind DNA. Mutations affecting transformation also impair the DNA-binding ability of these myb proteins.

    Area of Science:

    • Molecular Biology
    • Virology
    • Oncology

    Background:

    • Avian myeloblastosis virus (AMV) and avian leukemia virus E26 (E26) encode oncogene proteins, p48v-myb and p135gag-myb-ets, respectively.
    • These proteins are primarily localized in the nucleus of bone marrow cells.

    Purpose of the Study:

    • To investigate the DNA-binding properties of AMV and E26 oncogene proteins.
    • To determine the relationship between the transforming ability of these proteins and their DNA-binding capacity.

    Main Methods:

    • Indirect immunofluorescence was used to determine protein localization.
    • Immunoaffinity chromatography with monoclonal antibodies was employed for protein purification.
    • In vitro DNA-binding assays were performed to assess protein-DNA interactions.

    Main Results:

    • Purified p48v-myb and p135gag-myb-ets proteins demonstrated DNA-binding activity in vitro.
    • Mutant p135gag-myb-ets proteins, temperature-sensitive for transformation, showed reduced or thermolabile DNA-binding.
    • Myb-specific antibodies inhibited the DNA binding of AMV and E26 oncogene proteins.

    Conclusions:

    • The myb oncogene plays a crucial role in both cellular transformation and the DNA-binding activity of its encoded proteins.
    • Lesions within the myb oncogene directly impact its ability to interact with DNA.

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