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Related Experiment Videos

Dimer-dimer interfaces of the lambda-repressor are different in liganded and free states

S Bandyopadhyay1, C Mukhopadhyay, S Roy

  • 1Department of Biophysics, Bose Institute, Calcutta, India.

Biochemistry
|April 16, 1996
PubMed
Summary

Lambda repressor protein forms tetramers and higher structures through dimer-dimer interactions. Operator binding significantly alters the dimer-dimer interface, affecting protein association thermodynamics.

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Protein Structure and Dynamics

Background:

  • Lambda repressor protein regulates viral gene expression by binding to operator DNA.
  • Dimer-dimer interactions are critical for cooperative DNA binding and protein assembly.
  • Understanding the conformational changes upon operator binding is key to elucidating regulatory mechanisms.

Purpose of the Study:

  • To investigate the structural and thermodynamic changes in lambda repressor protein upon operator binding.
  • To characterize the dimer-dimer interface in both free and operator-bound states.
  • To determine the role of operator binding in modulating repressor association.

Main Methods:

  • Fluorescence quenching studies using tryptophan fluorescence and acrylodan labeling.

Related Experiment Videos

  • Thermodynamic measurements of protein association using fluorescence anisotropy.
  • Analysis of repressor oligomerization states (dimer, tetramer, octamer).

    • Main Results:

    • The tryptophan 230 environment differs significantly between unliganded and operator-bound repressor tetramers.
    • Acrylodan labeling at Cys 235 also reveals distinct environments in different repressor states.
    • Free repressor dimer association is enthalpy-driven, while operator-bound dimer association is entropy-driven.
    • Operator binding induces significant changes in the lambda repressor dimer-dimer interface.

    Conclusions:

    • The lambda repressor dimer-dimer interface undergoes substantial alterations upon operator binding.
    • Operator binding is crucial in modulating the nature of the dimer-dimer interface and repressor association thermodynamics.
    • These findings provide insights into the allosteric regulation of lambda repressor function.