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Heteromeric interactions among nucleoid-associated bacterial proteins: localization of StpA-stabilizing regions in H-NS of Escherichia coli.
Umeå University, Faculty of Medicine, Microbiology.
Umeå University, Faculty of Medicine, Microbiology.
Umeå University, Faculty of Medicine, Microbiology.
Umeå University, Faculty of Medicine, Microbiology.
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2001 (English)In: Journal of Bacteriology, ISSN 0021-9193, E-ISSN 1098-5530, Vol. 183, no 7, 2343-2347 p.Article in journal (Refereed) Published
Abstract [en]

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, StpA(F21C), forms dimers, whereas wild-type StpA in the absence of H-NS predominantly forms tetramers or oligomers, which are more susceptible to proteolysis.

Place, publisher, year, edition, pages
2001. Vol. 183, no 7, 2343-2347 p.
National Category
Microbiology in the medical area
Identifiers
URN: urn:nbn:se:umu:diva-33374DOI: 10.1128/JB.183.7.2343-2347.2001PubMedID: 11244076OAI: oai:DiVA.org:umu-33374DiVA: diva2:311650
Available from: 2010-04-22 Created: 2010-04-22 Last updated: 2017-12-12Bibliographically approved

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CiteExportLink to record
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