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Immunoassay for sequence-specific DNA-protein interaction.

R McKay

    Methods in Enzymology
    |January 1, 1983
    PubMed
    Summary
    This summary is machine-generated.

    This study introduces a new immunoassay to quantify DNA-protein interactions. The assay successfully identified Simian virus 40 (SV40) sequences binding T antigen, aiding in DNA-binding protein discovery.

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    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Virology

    Background:

    • Quantitative assays are crucial for studying DNA-protein interactions.
    • Understanding Simian virus 40 (SV40) T-antigen binding sites is key to viral replication and host cell manipulation.
    • Previous methods for identifying DNA-binding sites were limited.

    Purpose of the Study:

    • To develop and apply a novel immunoassay for quantifying DNA and specific DNA-binding protein interactions.
    • To determine the size and location of SV40 sequences that bind the viral T antigen.
    • To assess the assay's utility in detecting specific DNA-binding proteins in complex cellular extracts.

    Main Methods:

    • Utilized a previously described quantitative immunoassay.
    • Employed new DNase protection and footprinting procedures to map T-antigen binding sites on SV40 DNA.

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  • Tested the assay's sensitivity with crude protein extracts from SV40-transformed cell lines.

    • Main Results:

    • The immunoassay successfully quantified DNA-T antigen interactions.
    • New DNase protection and footprinting methods precisely mapped the size and location of T-antigen binding sites on SV40 DNA.
    • The assay detected specific DNA-binding proteins in crude extracts from SV40-transformed cells, even with a single viral genome copy.

    Conclusions:

    • The developed immunoassay is effective for quantitative analysis of DNA-protein interactions.
    • The method accurately identifies and characterizes DNA-binding sites for viral proteins like SV40 T antigen.
    • This procedure shows significant potential for identifying and purifying specific DNA-binding proteins from eukaryotic cells.