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Applied and Environmental Microbiology, December 2008, p. 7821-7823, Vol. 74, No. 24
0099-2240/08/$08.00+0     doi:10.1128/AEM.02028-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Influence of High Pressure on the Dimerization of ToxR, a Protein Involved in Bacterial Signal Transduction{triangledown}

Kai Linke,1 Nagarajan Periasamy,2 Matthias Ehrmann,1 Roland Winter,2 and Rudi F. Vogel1*

Technische Universität München, Lehrstuhl für Technische Mikrobiologie, 85350 Freising, Germany,1 Dortmund University of Technology, Physical Chemistry I—Biophysical Chemistry, D-44227 Dortmund, Germany2

Received 2 September 2008/ Accepted 10 October 2008

High hydrostatic pressure (HHP) is suggested to influence the structure and function of membranes and/or integrated proteins. We demonstrate for the first time HHP-induced dimer dissociation of membrane proteins in vivo with Vibrio cholerae ToxR variants in Escherichia coli reporter strains carrying ctx::lacZ fusions. Dimerization ceased at 20 to 50 MPa depending on the nature of the transmembrane segments rather than on changes in the ToxR lipid bilayer environment.

* Corresponding author. Mailing address: Lehrstuhl für Technische Mikrobiologie, Technische Universität München, Weihenstephaner Steig 16, 85350 Freising, Germany. Phone: 49 8161 713663. Fax: 49 8161 713327. E-mail: rudi.vogel{at}wzw.tum.de

{triangledown} Published ahead of print on 17 October 2008.

Applied and Environmental Microbiology, December 2008, p. 7821-7823, Vol. 74, No. 24
0099-2240/08/$08.00+0     doi:10.1128/AEM.02028-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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