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Related Experiment Videos

The efficiency of mispaired ligations by lambda integrase is extremely sensitive to context.

Sang Yeol Lee1, Arthur Landy

  • 1Division of Biology and Medicine, Brown University, Box G-J360, Providence, RI 02912, USA.

Journal of Molecular Biology
|September 15, 2004
PubMed
Summary

Phage lambda integrase (Int) protein

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Integrase (Int) protein from phage lambda is a key member of the tyrosine recombinase family.
  • This family performs DNA cleavage and ligation via a 3' phosphotyrosine intermediate to form and resolve Holliday junctions.

Purpose of the Study:

  • To investigate the mechanistic details of DNA cleavage and ligation by phage lambda integrase.
  • To compare the function of wild-type Int with a mutant (R169D) affecting protein complex formation.

Main Methods:

  • Development of a novel assay utilizing DNA hairpin formation to detect transient Int cleavage events.
  • Comparative analysis of wild-type and R169D mutant Int activity using the developed assay and other methods.

Main Results:

  • Wild-type Int's bottom-strand DNA cleavage efficiency is sensitive to the top-strand base pair, unlike the R169D mutant.
  • The R169D mutant exhibits faster hairpin formation with mispaired bases in multimeric complexes.
  • Wild-type Int's Holliday junction resolution is sensitive to ligation site homology, while the R169D mutant is not.

Conclusions:

  • The tetrameric integrase complex remains intact throughout Holliday junction resolution, including post-ligation.
  • This finding challenges models where DNA cleavage triggers complex dissociation during recombination resolution.

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