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Related Experiment Videos

Recognition of core-type DNA sites by lambda integrase

R S Tirumalai1, H J Kwon, E H Cardente

  • 1Department of Biology and Medicine, Brown University Providence, RI 02912, USA.

Journal of Molecular Biology
|June 26, 1998
PubMed
Summary
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The central domain of Escherichia coli phage lambda integrase (Int) is crucial for binding to core DNA sites. This binding is specific and autonomous, involving key amino acids like Lys103, Ala125, and Ala126.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Escherichia coli phage lambda integrase (Int) is a site-specific recombinase essential for phage DNA integration.
  • Int functions through distinct domains: an amino-terminal domain for arm-type DNA binding and a carboxy-terminal domain (C65) for core-type DNA binding, cleavage, and ligation.

Purpose of the Study:

  • To investigate the critical features of lambda Int binding to core-type DNA sites.
  • To elucidate the specific role of the central domain (residues 65-169) in DNA binding and recombination.

Main Methods:

  • Studied Int C65 fragment to simplify analysis of core-type DNA interactions.
  • Employed zero-length UV crosslinking to identify amino acids in close proximity to DNA.
  • Used pyridoxal 5'-phosphate modification to pinpoint residues at the protein-DNA interface.

Related Experiment Videos

Main Results:

  • Identified Ala125 and Ala126 through UV crosslinking as making close contact with core-type DNA.
  • Identified Lys103 via chemical modification as being at the protein-DNA interface.
  • The central domain (65-169) was cloned, purified, and demonstrated autonomous and specific binding to core-type DNA.

Conclusions:

  • The central domain of lambda Int, also termed the core-binding (CB) domain, plays a critical role in the specific and autonomous binding to core-type DNA sites.
  • Key residues Lys103, Ala125, and Ala126 within this domain are essential for protein-DNA interaction.
  • This highlights the synergistic roles of the catalytic and core-binding domains in the DNA binding and recombination process for Int and related enzymes.