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Related Experiment Videos

Interactions between DNA-bound repressors govern regulation by the lambda phage repressor.

A D Johnson, B J Meyer, M Ptashne

    Proceedings of the National Academy of Sciences of the United States of America
    |October 1, 1979
    PubMed
    Summary
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    Lambda phage repressor exhibits cooperative DNA binding at operator sites, with interactions shifting based on operator mutations. These cooperative binding events are crucial for regulating gene expression in lysogens.

    Area of Science:

    • Molecular Biology
    • Genetics
    • Biochemistry

    Background:

    • Bacteriophage lambda repressor protein controls gene expression by binding to operator DNA sequences.
    • The right operator (O(R)) contains three binding sites (O(R)1, O(R)2, O(R)3) for the repressor.
    • Repressor binding can be cooperative, meaning the binding of one repressor molecule influences the binding of another.

    Purpose of the Study:

    • To investigate the cooperative binding patterns of lambda phage repressor to the O(R) sites.
    • To elucidate the role of repressor-repressor interactions in modulating DNA binding affinity and gene regulation.
    • To understand how operator mutations alter repressor binding and downstream gene expression.

    Main Methods:

    • In vivo experiments were conducted to assess repressor binding and gene expression.

    Related Experiment Videos

  • Comparative analysis of repressor binding to wild-type and mutant O(R) DNA sequences.
  • Investigation of protein-protein contacts between repressor dimers using isolated domains.

    • Main Results:

    • Wild-type O(R) shows coordinate binding of repressor to O(R)1 and O(R)2, with O(R)3 binding at higher concentrations.
    • Mutant O(R)1 results in coordinate binding of O(R)2 and O(R)3, altering site affinities.
    • Repressor interactions are mediated by protein-protein contacts between adjacent dimers, as isolated domains bind non-cooperatively.
    • The cro protein, recognizing the same sites, binds non-cooperatively.

    Conclusions:

    • Lambda repressor binding is cooperative and context-dependent, influenced by operator sequence and repressor concentration.
    • Alternative protein-protein interactions between repressor dimers at O(R) sites dictate binding patterns and gene regulation.
    • Deletion of O(R)1 can switch repressor's effect from gene activation to repression, highlighting the importance of cooperative interactions.