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A structural basis for allosteric control of DNA recombination by lambda integrase.

Tapan Biswas1, Hideki Aihara, Marta Radman-Livaja

  • 1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.

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|June 24, 2005
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Site-specific DNA recombination, essential for cellular functions, is mediated by bacteriophage lambda integrase (lambda-int). Crystal structures reveal how lambda-int complexes with DNA substrates and regulatory DNA dictate recombination steps and favor product formation.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Site-specific DNA recombination is crucial for cellular processes like viral integration and gene regulation.
  • Bacteriophage lambda uses integrase (lambda-int) for integrating/excising its genome from the host chromosome.
  • This process involves lambda-int, accessory DNA sites, and regulatory proteins.

Purpose of the Study:

  • To elucidate the structural mechanisms of bacteriophage lambda site-specific DNA recombination.
  • To understand how lambda-int interacts with DNA substrates and regulatory elements.
  • To reveal how these interactions regulate the recombination pathway.

Main Methods:

  • X-ray crystallography was used to determine the structures of lambda-int in complex with DNA.
  • Structures captured various intermediates of the recombination reaction pathway.
  • Analysis focused on higher-order complexes involving substrates and regulatory DNAs.

Main Results:

  • Crystal structures revealed how lambda-int binds simultaneously to DNA via two domains, facilitating synapsis.
  • The structures illustrate the ordered DNA strand cleavage and exchange process.
  • Intertwined amino-terminal domains bound to accessory DNAs shape the complex, favoring recombinant products.

Conclusions:

  • The structures provide atomic-level insights into the mechanism of lambda site-specific recombination.
  • Simultaneous DNA binding by lambda-int domains is key to synapsis and reaction progression.
  • Accessory DNA binding by lambda-int influences the reaction equilibrium towards product formation.