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Related Experiment Videos

Kinetic studies on Cro repressor-operator DNA interaction.

J G Kim1, Y Takeda, B W Matthews

  • 1Laboratory of Molecular Biology, National Cancer Institute, Bethesda, MD 20892.

Journal of Molecular Biology
|July 5, 1987
PubMed
Summary
This summary is machine-generated.

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Cro repressor binds phage lambda operators with varying affinities, primarily affecting dissociation, not association. This interaction occurs via a DNA sliding mechanism, as supported by kinetic data and theoretical models.

Area of Science:

  • Molecular Biology
  • Biophysics
  • Genetics

Background:

  • Phage lambda utilizes six operators and a consensus sequence for gene regulation.
  • Cro repressor protein plays a key role in controlling phage lambda's lytic cycle.
  • Understanding repressor-operator interactions is crucial for deciphering gene expression control.

Purpose of the Study:

  • To synthesize and characterize the binding interactions of phage lambda operators with Cro repressor.
  • To elucidate the kinetic and thermodynamic parameters governing Cro repressor-operator DNA binding.
  • To investigate the mechanism by which Cro repressor locates and dissociates from its operator sites.

Main Methods:

  • Synthesis of 21 base-pair DNA fragments representing phage lambda operators and consensus sequence.

Related Experiment Videos

  • Filter binding assays to measure equilibrium dissociation constants (KD) and competition experiments for complex stability (t1/2).
  • Measurement of association rate constants (ka) and kinetic parameters for varying DNA fragment lengths.

    • Main Results:

    • Cro repressor exhibits highest affinity for the consensus operator (KD = 1.2 x 10(-12) M) and OR3 operator (KD = 2.0 x 10(-12) M).
    • Sequence variations in operators significantly impact dissociation rates (KD, kd) but not association rates (ka).
    • Cro repressor binding affinity is independent of DNA length, while association/dissociation rates increase with DNA length, supporting a sliding mechanism.

    Conclusions:

    • Cro repressor binding affinity is primarily determined by dissociation kinetics, not association kinetics.
    • The interaction of Cro repressor with its operator sites follows a two-step mechanism involving facilitated transfer.
    • Data strongly suggest that Cro repressor locates and dissociates from operators via a DNA sliding mechanism.