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Journal of Bacteriology, April 2001, p. 2343-2347, Vol. 183, No. 7
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.7.2343-2347.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Heteromeric Interactions among Nucleoid-Associated Bacterial Proteins: Localization of StpA-Stabilizing Regions in H-NS of Escherichia coli

Jörgen Johansson,dagger Sven Eriksson, Berit Sondén, Sun Nyunt Wai, and Bernt Eric Uhlin*

Department of Microbiology, Umeå University, S-90187 Umeå, Sweden

Received 28 August 2000/Accepted 8 January 2001

The nucleoid-associated proteins H-NS and StpA in Escherichia coli bind DNA as oligomers and are implicated in gene regulatory systems. There is evidence for both homomeric and heteromeric H-NS-StpA complexes. The two proteins show differential turnover, and StpA was previously found to be subject to protease-mediated degradation by the Lon protease. We investigated which regions of the H-NS protein are able to prevent degradation of StpA. A set of truncated H-NS derivatives was tested for their ability to mediate StpA stability and to form heteromers in vitro. The data indicate that H-NS interacts with StpA at two regions and that the presence of at least one of the H-NS regions is necessary for StpA stability. Our results also suggest that a proteolytically stable form of StpA, StpAF21C, forms dimers, whereas wild-type StpA in the absence of H-NS predominantly forms tetramers or oligomers, which are more susceptible to proteolysis.

* Corresponding author. Mailing address: Department of Microbiology, Umeå University, S-90187 Umeå, Sweden. Phone: 46-90-7856731. Fax: 46-90-772630. E-mail: Bernt.Eric.Uhlin{at}micro.umu.se.

dagger Present address: Unité des Interactions Bactéries-Cellules, Institut Pasteur, 75724 Paris Cedex 15, France.

Journal of Bacteriology, April 2001, p. 2343-2347, Vol. 183, No. 7
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.7.2343-2347.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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