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Related Experiment Videos

lambda Rap protein is a structure-specific endonuclease involved in phage recombination

G J Sharples1, L M Corbett, I R Graham

  • 1Institute of Genetics, University of Nottingham, Queens Medical Centre, Nottingham NG7 2UH, United Kingdom.

Proceedings of the National Academy of Sciences of the United States of America
|November 13, 1998
PubMed
Summary

The bacteriophage lambda Rap protein, essential for DNA repair, acts as an endonuclease. It preferentially binds and cleaves branched DNA structures like Holliday junctions, offering insights into DNA recombination mechanisms.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Bacteriophage lambda possesses genes crucial for DNA double-strand break repair.
  • The Rap protein is a key player in this recombinational repair pathway.

Purpose of the Study:

  • To purify and biochemically characterize the bacteriophage lambda Rap protein.
  • To elucidate the role of Rap in DNA repair and recombination.

Main Methods:

  • Purification of the Rap protein.
  • Analysis of Rap binding to branched DNA substrates (Holliday junctions, D-loops).
  • Enzymatic assays to determine Rap's endonuclease activity.

Main Results:

  • Full-length and truncated Rap proteins were purified.

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  • Rap preferentially binds to branched DNA structures.
  • Rap functions as a manganese-dependent endonuclease, cleaving at the branch point of Holliday junctions and D-loops without sequence preference.

    • Conclusions:

    • Rap's endonuclease activity on branched DNA provides a mechanism for generating recombinants.
    • This activity may occur without the formation of a classical Holliday junction, offering a novel insight into DNA recombination.