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J Bacteriol, February 1998, p. 994-997, Vol. 180, No. 4
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The StpA Protein Functions as a Molecular Adapter To Mediate Repression of the bgl Operon by Truncated H-NS in Escherichia coli

Andrew Free,1,* Roy M. Williams,2,dagger and Charles J. Dorman1

Department of Microbiology, Moyne Institute of Preventive Medicine, Trinity College, Dublin 2, Republic of Ireland,1 and Unité de Physicochimie des Macromolécules Biologiques, Institut Pasteur, 75724 Paris Cedex 15, France2

Received 4 September 1997/Accepted 16 December 1997

The mechanism of repression of the beta -glucoside utilization (bgl) operon of Escherichia coli by a carboxy-terminally truncated derivative of the nucleoid-associated protein H-NS which is defective in DNA binding was investigated. The DNA-binding function of the H-NS-like protein StpA was found to be necessary for repression, which is consistent with a role for StpA as a DNA-binding adapter for mutant derivatives of H-NS.

* Corresponding author. Present address: Institute of Cell and Molecular Biology, University of Edinburgh, Darwin Building, Mayfield Rd., Edinburgh EH9 3JR, United Kingdom. Phone: 44-131-6508695. Fax: 44-131-6505379. E-mail: Andrew.Free{at}ed.ac.uk.

dagger Present address: Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 60637.




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