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Related Experiment Videos

Lambda repressor mutants that are better substrates for RecA-mediated cleavage.

F S Gimble1, R T Sauer

  • 1Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.

Journal of Molecular Biology
|March 5, 1989
PubMed
Summary
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New mutations in bacteriophage lambda repressor accelerate RecA-mediated cleavage. Poor dimer formation correlates with increased cleavage, supporting a monomer substrate model for this essential DNA repair pathway.

Area of Science:

  • Molecular Biology
  • Genetics

Background:

  • RecA-mediated cleavage of bacteriophage lambda repressor protein is a key step in prophage induction.
  • Understanding the factors influencing this cleavage is crucial for comprehending viral DNA regulation.

Purpose of the Study:

  • To identify mutations in lambda repressor that enhance RecA-mediated cleavage.
  • To elucidate the role of repressor dimerization in RecA-mediated cleavage.

Main Methods:

  • Isolation of intragenic second-site suppressor mutations in lambda repressor.
  • Biochemical assays using purified repressor proteins to assess RecA-mediated cleavage rates.
  • Analysis of repressor dimerization properties.

Main Results:

  • Three lambda repressor mutations were identified that significantly increase RecA-mediated cleavage rates.

Related Experiment Videos

  • Mutations enhancing cleavage also impaired repressor dimerization.
  • A covalently linked repressor dimer showed resistance to cleavage, indicating monomers are the preferred substrate.

    • Conclusions:

    • Repressor monomers, not dimers, are the primary substrate for RecA-mediated cleavage.
    • Dimerization state significantly influences the susceptibility of lambda repressor to RecA-mediated cleavage.