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Journal of Bacteriology, July 2005, p. 4752-4759, Vol. 187, No. 14
0021-9193/05/$08.00+0     doi:10.1128/JB.187.14.4752-4759.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Chill Activation of Compatible Solute Transporters in Corynebacterium glutamicum at the Level of Transport Activity

Nuran Özcan, Reinhard Krämer,* and Susanne Morbach

Institute of Biochemistry, University of Cologne, Cologne, Germany

Received 29 November 2004/ Accepted 15 April 2005

The gram-positive soil bacterium Corynebacterium glutamicum harbors four osmoregulated secondary uptake systems for compatible solutes, BetP, EctP, LcoP, and ProP. When reconstituted in proteoliposomes, BetP was shown to sense hyperosmotic conditions via the increase in luminal K+ and to respond by instant activation. To study further putative ways of stimulus perception and signal transduction, we have investigated the responses of EctP, LcoP, and BetP, all belonging to the betaine-carnitine-choline transporter family, to chill stress at the level of activity. When fully activated by hyperosmotic stress, they showed the expected increase of activity at increasing temperature. In the absence of osmotic stress, EctP was not activated by chill and LcoP to only a very low extent, whereas BetP was significantly stimulated at low temperature. BetP was maximally activated at 10°C, reaching the same transport rate as that observed under hyperosmotic conditions at this temperature. A role of cytoplasmic K+ in chill-dependent activation of BetP was ruled out, since (i) the cytoplasmic K+ concentration did not change significantly at lower temperatures and (ii) a mutant BetP lacking the C-terminal 25 amino acids, which was previously shown to have lost the ability to be activated by luminal K+, was fully competent in chill sensing. When heterologously expressed in Escherichia coli, BetP did not respond to chill stress. This may indicate that the membrane in which BetP is inserted plays an important role in chill activation and thus in signal transduction by BetP, different from the previously established K+-mediated process.


* Corresponding author. Mailing address: Institute of Biochemistry, University of Cologne, Zülpicher Str. 47, 50674 Köln, Germany. Phone: 49 221 470 6461. Fax: 49 221 470 5091. E-mail: r.kraemer{at}uni-koeln.de.


Journal of Bacteriology, July 2005, p. 4752-4759, Vol. 187, No. 14
0021-9193/05/$08.00+0     doi:10.1128/JB.187.14.4752-4759.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




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