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Related Experiment Video

Updated: May 5, 2026

Amplification, Next-generation Sequencing, and Genomic DNA Mapping of Retroviral Integration Sites
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Autonomous DNA binding domains of lambda integrase recognize two different sequence families.

L Moitoso de Vargas1, C A Pargellis, N M Hasan

  • 1Division of Biology and Medicine, Brown University, Providence, Rhode Island 02912.

Cell
|September 23, 1988
PubMed
Summary

The lambda Integrase protein has two independent DNA-binding domains. These domains recognize different DNA sequences and can bind simultaneously, suggesting a role in linking DNA segments.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Protein Biochemistry

Background:

  • The lambda Integrase protein (Int) is crucial for site-specific recombination in bacteriophage lambda.
  • Understanding its DNA-binding properties is key to elucidating its mechanism of action.

Purpose of the Study:

  • To investigate the DNA-binding domains of the 40 kd lambda Integrase protein.
  • To determine the sequence specificities and functional independence of these domains.

Main Methods:

  • Nuclease protection assays to study Int binding activity.
  • Proteolytic cleavage of Int followed by footprinting analysis.
  • Physical separation and characterization of DNA-binding peptides.

Main Results:

  • The 40 kd lambda Integrase protein possesses two autonomous DNA-binding domains.
  • An amino-terminal peptide binds to "arm-type" sites, while a carboxy-terminal peptide binds to "core-type" sequences.
  • These domains exhibit distinct sequence specificities and can function independently.

Conclusions:

  • The lambda Integrase protein has two functionally independent DNA-binding domains.
  • The ability of these domains to bind simultaneously supports a model where Integrase links disparate DNA sequences.