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Related Experiment Videos

Complementation of bacteriophage lambda integrase mutants: evidence for an intersubunit active site

Y W Han1, R I Gumport, J F Gardner

  • 1Department of Microbiology, College of Medicine, University of Illinois at Urbana-Champaign 61801.

The EMBO Journal
|December 1, 1993
PubMed
Summary

Bacteriophage lambda site-specific recombination involves intasomes. Two integrase (Int) monomers are necessary for catalytic cleavage at the B site, forming the active site during recombination.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Site-specific recombination is crucial for bacteriophage lambda replication.
  • Recombination initiates with higher-order protein-DNA complexes called intasomes.
  • Intasomes, like the attL complex, involve phage integrase (Int), integration host factor (IHF), and attL DNA.

Purpose of the Study:

  • To investigate the mechanism of DNA cleavage during bacteriophage lambda site-specific recombination.
  • To determine the role of integrase (Int) monomers in forming the catalytically active species.

Main Methods:

  • In vitro complementation assays using attL suicide substrates.
  • Site-directed mutagenesis of conserved residues in integrase (Int).
  • Analysis of DNA cleavage at the B site in the presence of mutant Int proteins.

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Main Results:

  • At least two Int monomers are required for catalytically competent cleavage at the B site.
  • The Tyr342 residue of Int is essential for nucleophilic attack during strand cleavage.
  • Mutagenesis studies identified key residues involved in the catalytic activity of Int.

Conclusions:

  • The active site for DNA cleavage in bacteriophage lambda recombination is likely formed by two Int monomers.
  • Understanding intasome formation and function is key to elucidating the recombination mechanism.