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Related Experiment Videos

Core-binding specificity of bacteriophage integrases.

P Gottfried1, E Yagil, M Kolot

  • 1Department of Biochemistry, The George S. Wise Center for Life Sciences, Tel-Aviv University, Israel.

Molecular & General Genetics : MGG
|June 14, 2000
PubMed
Summary

Bacteriophage integrase proteins, though homologous, exhibit specific DNA binding. This study reveals that differences in how integrases bind to att sites dictate the specificity of site-specific recombination in lambda and HK022 phages.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Virology

Background:

  • Site-specific recombination is crucial for bacteriophage lambda and HK022.
  • Their integrase proteins share homology but exhibit distinct att site specificity.

Purpose of the Study:

  • To investigate the molecular basis of integrase specificity in bacteriophage lambda and HK022.
  • To determine how integrase proteins differentiate between cognate and non-cognate att sites.

Main Methods:

  • Gel-retardation assays were used to examine DNA-protein complexes.
  • Interactions between integrase proteins and attL/attR sites from both phages were analyzed.

Main Results:

  • Each integrase formed higher-order complexes exclusively with its cognate att sites.

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  • Integrase proteins showed differential binding to att sites, indicating specificity is determined by DNA-protein interactions.

    • Conclusions:

    • The mode of integrase binding to the att core sequences is the primary determinant of specificity.
    • This binding difference explains the distinct recombination activities of lambda and HK022 integrases.