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Lac repressor - lac operator interaction. Circular dichroism study.

F Culard, J C Maurizot

    Nucleic Acids Research
    |October 10, 1981
    PubMed
    Summary
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    Lac repressor binding to operator DNA causes a distinct conformational change, unlike non-specific binding. Stoichiometry is complex, revealing a two operators-one repressor complex.

    Area of Science:

    • Molecular biology
    • Biophysics
    • Genetics

    Background:

    • The lac repressor protein regulates gene expression by binding to specific DNA operator sequences.
    • Understanding the precise molecular interactions between regulatory proteins and DNA is crucial for deciphering gene control mechanisms.

    Purpose of the Study:

    • To investigate the conformational changes in operator DNA upon binding with the lac repressor.
    • To determine the stoichiometry and nature of the lac repressor-operator DNA complex.

    Main Methods:

    • Circular dichroism (CD) spectroscopy was employed to monitor DNA conformation.
    • Gel filtration chromatography was used to assess the complex formation and stoichiometry.

    Main Results:

    Related Experiment Videos

  • Lac repressor binding induces a unique conformational change in operator DNA, distinct from non-specific DNA binding.
  • CD titration revealed a complex binding stoichiometry.
  • A 2:1 complex of operator DNA to lac repressor was identified and confirmed by gel filtration.

    • Conclusions:

    • The lac repressor interacts with operator DNA in a specific manner, inducing characteristic structural alterations.
    • The formation of a 2:1 operator-DNA:repressor complex suggests a unique binding mode for transcriptional regulation.