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Spectroscopic study of Y210C lambda-repressor: implications for cooperative interaction

S Deb1, S Bandyopadhyay, S Roy

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

Protein Engineering
|September 2, 1998
PubMed
Summary
This summary is machine-generated.

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A lambda-repressor mutant (Y210C) lacks cooperative DNA binding and shows weaker self-assembly. This suggests the internal C210 residue is crucial for protein function, likely by destabilizing a structural turn.

Area of Science:

  • Molecular Biology
  • Protein Biochemistry
  • Structural Biology

Background:

  • Lambda-repressor is a key protein regulating phage lambda DNA replication.
  • Understanding repressor protein interactions is crucial for gene regulation studies.

Purpose of the Study:

  • To characterize a non-cooperative lambda-repressor mutant (Y210C).
  • To investigate the structural and functional role of C210 in repressor activity.

Main Methods:

  • Protein purification and characterization.
  • Near-UV and far-UV circular dichroism (CD) spectroscopy.
  • Fluorescence anisotropy measurements.
  • Acrylamide quenching assays.

Main Results:

Related Experiment Videos

  • The Y210C mutant protein demonstrated no cooperative DNA binding.
  • Mutant protein exhibited significantly weaker self-assembly.
  • Far-UV CD spectra indicated a structural change in the mutant protein.
  • Operator-induced conformational changes were preserved in the Y210C mutant.

    • Conclusions:

    • Cysteine 210 (C210) is located internally and is essential for cooperative interactions.
    • The Y210C mutation likely affects protein function by destabilizing a reverse turn structure.
    • This study provides insights into the structural basis of cooperativity in lambda-repressor.