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Related Experiment Videos

Genetic analysis of the bacteriophage lambda attL nucleoprotein complex

M P MacWilliams1, R I Gumport, J F Gardner

  • 1Department of Microbiology, University of Illinois, Urbana 61801, USA.

Genetics
|July 1, 1996
PubMed
Summary

Bacteriophage lambda integrase (Int) and integration host factor (IHF) form DNA complexes. Conserved amino acids in Int are crucial for binding lambda core sites, impacting DNA recombination.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Site-specific recombination is essential for bacteriophage lambda DNA integration and excision.
  • This process involves complex interactions between integrase (Int) and integration host factor (IHF).

Purpose of the Study:

  • To analyze the elements required for forming an in vivo nucleoprotein complex of Int and IHF.
  • To characterize Int variants and their roles in binding lambda attL sites.

Main Methods:

  • In vivo attL binding assay was used to study Int-core binding.
  • Site-directed mutagenesis was employed to create Int variants with specific amino acid substitutions.

Main Results:

  • Int-core binding is stabilized by the attL arm region and requires IHF.

Related Experiment Videos

  • Substitution of tyrosine 342 in Int did not affect attL complex formation.
  • Mutations in conserved residues (arginine 212, histidine 308, arginine 311) altered attL complex formation while preserving binding to arm-type sites.

    • Conclusions:

    • A triad of conserved amino acids in Int is critical for interaction with lambda core sites.
    • These residues contribute to DNA binding beyond their catalytic function in recombination.