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Journal of Bacteriology, September 2002, p. 5200-5203, Vol. 184, No. 18
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.18.5200-5203.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Interactions between Integrase and Excisionase in the Phage Lambda Excisive Nucleoprotein Complex

Department of Science Education, Chosun University, Kwangju, Korea,¹ Department of Biochemistry and College of Medicine,² Department of Microbiology, University of Illinois, Urbana, Illinois³

Received 21 March 2002/ Accepted 12 June 2002

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 -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.

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