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Multiple repressor binding at the operators in bacteriophage lambda.

T Maniatis, M Ptashne

    Proceedings of the National Academy of Sciences of the United States of America
    |May 1, 1973
    PubMed
    Summary
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    Lambda repressor protein protects short DNA fragments at operator sites. Increasing repressor levels reveals six protected DNA fragments, indicating sequential binding at lambda operators.

    Area of Science:

    • Molecular Biology
    • Genetics
    • Biochemistry

    Background:

    • Bacteriophage lambda repressor protein regulates viral gene expression.
    • Lambda repressor binds to specific DNA sequences called operators (o(L) and o(R)).
    • Understanding repressor-operator interactions is crucial for gene regulation studies.

    Purpose of the Study:

    • To investigate the binding mechanism of lambda repressor to its operator DNA sequences.
    • To characterize the DNA fragments protected by lambda repressor.
    • To determine the order and nature of repressor binding events.

    Main Methods:

    • Nuclease digestion of lambda DNA in the presence of varying lambda repressor concentrations.
    • Isolation and size determination of protected DNA fragments.

    Related Experiment Videos

  • Analysis of nucleotide sequences and repressor binding affinities.

    • Main Results:

    • Six successively larger DNA fragments (35-100 bp) were protected by lambda repressor at both o(L) and o(R).
    • Repressor binding occurred at a unique site first, followed by sequential filling of five additional sites.
    • o(L) and o(R) have distinct nucleotide sequences and repressor affinities.
    • No evidence for hairpin structures or DNA unwinding upon repressor binding was found.

    Conclusions:

    • Lambda repressor binding to operators is a sequential, directional process.
    • The protected fragments provide insights into the precise binding sites and stoichiometry.
    • The operator DNA remains double-stranded and does not form hairpin structures during repressor interaction.