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Structure-function analysis of IntDOT.

Seyeun Kim1, Brian M Swalla, Jeffrey F Gardner

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

Journal of Bacteriology
|November 17, 2009
PubMed
Summary
This summary is machine-generated.

CTnDOT integrase (IntDOT) facilitates recombination between different DNA sequences. Mutational analysis revealed novel roles for its N-terminal domain and identified Arg-285 as a unique catalytic residue, suggesting a new active-site mechanism.

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Area of Science:

  • Molecular Biology
  • Enzymology
  • Genetics

Background:

  • CTnDOT integrase (IntDOT) is a tyrosine family site-specific DNA recombinase.
  • IntDOT uniquely catalyzes recombination between nonidentical DNA sequences.
  • Previous studies focused on catalytic (CAT) and core-binding (CB) domains, noting a missing active-site residue (Arg I) and CB domain involvement.

Purpose of the Study:

  • To identify mutations disrupting IntDOT's in vivo integrative recombination using a genetic screen.
  • To characterize the DNA binding, cleavage, and ligation activities of IntDOT mutants.
  • To elucidate the functional roles of IntDOT domains and active-site residues.

Main Methods:

  • Constructed an Escherichia coli indicator strain for screening IntDOT mutations.
  • Isolated and characterized 25 IntDOT mutants for recombination activities.
  • Employed biochemical assays, mutational analysis, and homology modeling.

Main Results:

  • Mutants with N-domain substitutions were catalytically active but impaired in nucleoprotein complex formation.
  • Ala-352 substitution in the CAT domain disrupted DNA cleavage but not ligation, implicating it in catalytic tyrosine positioning.
  • Arg-285 was identified as the missing Arg I residue, with a unique active-site entry point.

Conclusions:

  • The N-domain of IntDOT is crucial for DNA binding and/or protein-protein interactions.
  • Ala-352 plays a specific role in the DNA cleavage step of recombination.
  • IntDOT possesses a novel active-site architecture, with Arg-285 utilizing an unusual binding mode for catalysis.