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Nucleic Acids Research, 1992, Vol. 20, No. 10 2525-2532
© 1992

MOLECULAR BIOLOGY

Purification and characterization of TnsC, a Tn7 transposition protein that binds ATP and DNA

Pascal Gamas+ and Nancy L. Craig*

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

* To whom correspondence should be addressed at Howard Hughes Medical Institute and Department of Molecular Biology & Genetics, 615 PCTB, Johns Hopkins School of Medicine, 725 N. Wolfe Street, Baltimore MD 21205–2185, USA

Received January 21, 1992. Revised April 9, 1992. Accepted April 9, 1992.

The bacterial transposon Tn7 encodes five transposition genes tnsABCDE. We report a simple and rapid procedure for the purification of TnsC protein. We show that purified TnsC is active in and required for Tn7 transposition in a cell-free recombination system. This finding demonstrates that TnsC participates directly in Tn7 transposition and explains the requirement for tnsC function in Tn7 transposition. We have found that TnsC binds adenine nucleotides and is thus a likely site of action of the essential ATP cofactor in Tn7 transposition. We also report that TnsC binds non-specifically to DNA in the presence of ATP or the generally non-hydrolyzable analogues AMP-PNP and ATP-{gamma}-S, and that TnsC displays little affinity for DNA in the presence of ADP. We speculate that TnsC plays a central role in the selection of target DNA during Tn7 transposition.

+ Present address: Laboratoire de Biologie Moleculaire des Relations Plantes-Microorganismes, CNRS-INRA, BP27-31326, Castanet Tolosan Cedex, France


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