PMID:11244076

Citation	Johansson, J, Eriksson, S, Sondén, B, Wai, SN and Uhlin, BE (2001) Heteromeric interactions among nucleoid-associated bacterial proteins: localization of StpA-stabilizing regions in H-NS of Escherichia coli. J. Bacteriol. 183:2343-7
Abstract	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.
Links	PubMed PMC95143 Online version:10.1128/JB.183.7.2343-2347.2001
Keywords	Bacterial Proteins; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/physiology; Dimerization; Escherichia coli/chemistry; Escherichia coli Proteins; Molecular Chaperones
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