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Nucleic Acids Research, 1991, Vol. 19, No. 12 3395-3402
© 1991

MOLECULAR BIOLOGY

Purification and characterisation of the TnsB protein of Tn7: a transposition protein that binds to the ends of Tn7

Yue Tang, Conrad Lichtenstein1 and Sue Cotterill*

Department of Biochemistry, Imperial College of Science, Technology & Medicine Exhibition Road, London SW7 2AZ, UK 1Center for Biotechnology, Imperial College of Science, Technology & Medicine Exhibition Road, London SW7 2AZ, UK

* To whom correspondence should be addressed

Received February 4, 1991. Revised March 28, 1991. Accepted March 28, 1991.

Tn7, a large bacterial transposon encodes 5 proteins required for its transposition. We report a rapid and easy purification of one of these proteins, TnsB, from an overexpression strain. This protein was shown to bind to the ends of Tn7, in a bandshift assay, in two distinct stages as a function of protein concentration. DNasel footprlntIng at each end of Tn7 showed that the TnsB recognition sequence, a set of 22 bp repeats, plus Tn7 terminl are protected. Binding of TnsB appeared cooperative but was only observed above a threshold concentration of protein. ATP and Mg2+ had no effect on the pattern of protection, nor did addition of other Tn7-encoded proteins. Hydroxyl radical footprinting, performed at the right end, showed that TnsB binds preferentially to one side of the DNA helix.


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