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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, 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 -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.

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^* 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.

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

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