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Related Experiment Videos

Probing the physical basis for trp repressor-operator recognition.

A O Grillo1, M P Brown, C A Royer

  • 1School of Pharmacy, University of Wisconsin-Madison, 425 N. Charter, Madison, WI, 53706, USA.

Journal of Molecular Biology
|March 27, 1999
PubMed
Summary
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The trp repressor binds DNA cooperatively, with specific base sequences dictating affinity and asymmetry. Mutations reveal key DNA elements controlling trp repressor binding specificity and affinity.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • The trp repressor is a well-studied transcriptional regulator.
  • Understanding its DNA operator recognition is crucial but incomplete.
  • Factors like co-repressor binding and DNA dynamics influence recognition.

Purpose of the Study:

  • To elucidate the structural and energetic basis of trp repressor-operator site recognition.
  • To define how operator DNA sequence elements control binding affinity and cooperativity.
  • To investigate the role of specific bases in trp repressor binding specificity.

Main Methods:

  • Studied trp repressor binding to mutated operator targets.
  • Utilized fluorescence anisotropy for high-quality binding data.

Related Experiment Videos

  • Estimated binding affinities and cooperativity.

    • Main Results:

    • Trp repressor exhibits slight cooperativity, forming 2:1 dimer/DNA complexes.
    • A third dimer binds with lower affinity, indicating target asymmetry.
    • Specific bases (GNACT sequence) are critical for binding specificity and affinity.
    • Mutations in key bases abolish specificity or significantly reduce affinity.

    Conclusions:

    • DNA sequence elements, particularly the GNACT half-site, are critical for trp repressor binding specificity and cooperativity.
    • Trp repressor binding is inherently asymmetric on its operator site.
    • Apo-repressor binding affinity is higher than holo-repressor binding to non-specific DNA.