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Lac repressor-Lac operator complexes. Solution X-ray scattering and electrophoretic studies.

F Culard, M Charlier, J C Maurizot

    European Biophysics Journal : EBJ
    |January 1, 1987
    PubMed
    Summary
    This summary is machine-generated.

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    Researchers studied Lac repressor and DNA operator complexes using gel electrophoresis and X-ray scattering. Two complexes were identified: one with one repressor and two operators, and another with four repressors and two operators.

    Area of Science:

    • Molecular Biology
    • Biophysics

    Background:

    • The Lac repressor protein regulates gene expression by binding to specific DNA operator sequences.
    • Understanding repressor-operator complex stoichiometry is crucial for elucidating gene regulation mechanisms.

    Purpose of the Study:

    • To characterize the stoichiometry and structure of complexes formed between the Lac repressor and a 29 base pair DNA operator fragment.
    • To investigate the binding behavior of Lac repressor to its operator using biophysical techniques.

    Main Methods:

    • Polyacrylamide gel electrophoresis (PAGE) for complex separation.
    • Solution X-ray scattering (SXS) to determine structural parameters like radii of gyration.

    Main Results:

    • PAGE revealed two distinct complexes at repressor/operator ratios of 0.5 and 2.

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  • X-ray scattering indicated a 1:2 repressor/operator complex and a 4:2 repressor/operator complex.
  • Equimolar mixing resulted in a heterogeneous mixture of both complex types.

    • Conclusions:

    • The Lac repressor can form distinct stoichiometric complexes with its operator DNA.
    • A structural model for the higher-order 4:2 complex was proposed, offering insights into cooperative binding or multimerization.