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Nucleic Acids Research, 1991, Vol. 19, No. 18 5021-5029
© 1991

MOLECULAR BIOLOGY

Interaction of the Tn7-encoded transposition protein TnsB with the ends of the transposon

Lidia K. Arciszewska1,3,+ and Nancy L. Craig1,2,3,*

1Department of Microbiology and Immunology San Francisco, CA 94143, USA 2Department of Biochemistry and Biophysics San Francisco, CA 94143, USA 3The George W. Hooper Foundation, University of California San Francisco, CA 94143, USA

*To whom correspondence should be addressed at HSW 1542, 3rd & Parnassus, University of California, San Francisco, CA 94143, USA

Received May 7, 1991. Accepted August 22, 1991.

We have used several high resolution methods to examine the interaction of TnsB, a transposition protein encoded by the bacterial transposon Tn7, with its binding sites at the ends of the transposon. These binding sites lie within the DNA segments that are directly involved in transposition. We show that the binding of TnsB to DNA can promote DNA bending, suggesting that the interaction of TnsB with the ends may result in formation of a highly organized protein-DNA complex. We also Identify likely positions of close contact between TnsB and its binding sites. Analysis of the interaction of TnsB with Intact Tn7 ends reveals TnsB occupies its binding sites in a particular order, the sites immediately adjacent to the transposon termini being occupied only after other inner sites are bound. Such ordered occupancy suggests that the various binding sites have differing apparent affinities for TnsB.

+Present address: University of Glasgow, Institute of Genetics, Glasgow, UK


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