Interactions between integrase and excisionase in the phage lambda excisive nucleoprotein complex
Related Experiment Video
Updated: Sep 29, 2026

Detection and Removal of Nuclease Contamination During Purification of Recombinant Prototype Foamy Virus Integrase
Published on: December 8, 2017
Eun Hee Cho1, Richard I Gumport, Jeffrey F Gardner
1Department of Science Education, Chosun University, Kwangju, Korea.
Abstract:
Bacteriophage lambda site-specific recombination comprises two overall reactions, integration into and excision from the host chromosome. Lambda integrase (Int) carries out both reactions. During excision, excisionase (Xis) helps Int to bind DNA and introduces a bend in the DNA that facilitates formation of the proper excisive nucleoprotein complex. The carboxyl-terminal alpha-helix of Xis is thought to interact with Int through direct protein-protein interactions. In this study, we used gel mobility shift assays to show that the amino-terminal domain of Int maintained cooperative interactions with Xis. This finding indicates that the amino-terminal arm-type DNA binding domain of Int interacts with Xis.
Related Concept Videos
Conservative Site-specific Recombination and Phase Variation
The recognition sites for Cre recombinase called LoxP...
DNA Bacteriophages
Homologous Recombination
Viral Replication: Lysogenic Cycle
Nucleotide Excision Repair
Nucleotide Excision Repair
Cells are regularly exposed to mutagens—factors in the environment that can damage DNA and generate mutations. UV radiation is one of the most common mutagens and is estimated to introduce a significant number of changes in DNA. These include bends or kinks in the structure, which can block DNA replication or transcription. If these errors are not fixed, the damage can cause mutations, which in turn can result in cancer or disease depending on which sequences are...

