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Related Experiment Videos

Conformational dynamics of a transposition repressor in modulating DNA binding.

S S Rai1, D O'Handley, H Nakai

  • 1Department of Biochemistry and Molecular Biology, Georgetown University Medical Center, Room 331 Basic Science Building, 3900 Reservoir Road NW, Washington, DC 20007, USA.

Journal of Molecular Biology
|September 14, 2001
PubMed
Summary

The bacteriophage Mu repressor

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Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • The bacteriophage Mu repressor protein is crucial for maintaining lysogeny.
  • It functions by binding to operator DNA and inhibiting transposition.
  • N-terminal domains are known for DNA binding, while C-terminal mutations can be suppressed by truncations.

Purpose of the Study:

  • To investigate the role of the C-terminal tail in the DNA binding of the bacteriophage Mu repressor.
  • To understand the conformational changes and interactions of the repressor during DNA binding.

Main Methods:

  • Fluorescent probe attachment to the C terminus to analyze its environment and movement.
  • Monitoring tryptophan fluorescence quenching to assess proximity between C terminus and DNA-binding domain.

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  • Trypsin digestion assays to identify hypersensitive sites and assess protein stability.

    • Main Results:

    • The C-terminal tail resides in a hydrophobic environment near the DNA-binding domain.
    • DNA interaction causes the tail to move away from the DNA-binding domain.
    • The tail's presence creates a trypsin-sensitive site in the DNA-binding domain, which is relieved by DNA binding.

    Conclusions:

    • The C-terminal tail of the bacteriophage Mu repressor sterically hinders DNA binding.
    • Conformational changes involving tail movement are essential for repression establishment and cooperative DNA binding.
    • These findings shed light on the dynamic regulation of bacteriophage DNA-protein interactions.