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Nucleic Acids Research, 1991, Vol. 19, No. 7 1399-1405
© 1991


MOLECULAR BIOLOGY

The C-terminal domain of the Escherichia coli DNA gyrase A subunit is a DNA-binding protein

Richard J. Reece+ and Anthony Maxwell*

Department of Biochemistry, University of Leicester University Road, Leicester LE1 7RH, UK

* To whom correspondence should be addressed

Received February 1, 1991. Revised February 28, 1991. Accepted February 28, 1991.

We have constructed a clone which over-produces a 33 kDa protein representing the C-termlnal portion of the Escherichia coli DNA gyrase A subunit. This protein has no enzymic activity of its own, but will form a complex with a 64 kDa protein (representing the N-terminal part of the A subunit) and the gyrase B subunit, that will efficiently catalyse DNA supercoiling. We show that the 33 kDa protein can bind to DNA on its own in a manner which induces positive supercoiling of the DNA. We propose that the 33 kDa protein represents a domain of the gyrase A subunit which is involved in the wrapping of DNA around DNA gyrase.


+ Present address: Department of Biochemistry and Molecular Biology, Harvard University, 7 Divinity Avenue, Cambridge, MA 02138, USA


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