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J Biol Chem, Vol. 275, Issue 2, 735-741, January 14, 2000

Osmosensor and Osmoregulator Properties of the Betaine Carrier BetP from Corynebacterium glutamicum in Proteoliposomes*

René RübenhagenDagger , Hendrik RönschDagger , Heinrich Jung§, Reinhard KrämerDagger , and Susanne MorbachDagger

From the Dagger  Institut für Biochemie, Universität zu Köln, Zülpicher Strabeta e 47, 50674 Köln, and the § Abteilung Mikrobiologie, Universität Osnabrück, Fachbereich Biologie/Chemie, 49069 Osnabrück, Germany

The secondary glycine betaine uptake system BetP of Corynebacterium glutamicum was purified from Escherichia coli membranes in strep-tagged form after heterologous expression of the betP gene and was reconstituted in E. coli lipids. BetP retained its kinetic properties (Vmax and Km for betaine and Na+) as compared with intact cells. The influence of driving forces (Na+ gradient and/or electrical potential) on betaine uptake was quantified in proteoliposomes. BetP was effectively regulated by the external osmolality and was stimulated by the local anesthetic tetracaine. A shift of the optimum of osmotic stimulation to higher osmolalities was linearly correlated with an increasing share of phosphatidyl glycerol, the major lipid of the C. glutamicum plasma membrane in the E. coli lipid proteoliposomes. This finding correlates with results demonstrating an identical shift when betP was expressed in E. coli instead of C. glutamicum. These data indicate that (i) BetP comprises all elements of osmosensing and osmoregulatory mechanisms of betaine uptake, (ii) osmoregulation of BetP is directly related to protein/membrane interactions, (iii) the turgor pressure presumably plays no major role in osmoregulation of BetP, and (iv) the regulatory properties of BetP may be related to the physical state of the surrounding membrane.

* This work was supported by a grant from the Deutsche Forschungsgemeinschaft (Schwerpunkt 1071) and by the Fonds der Chemischen Industrie.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 49 221 470 6461; Fax: 49 221 470 5091; E-mail: r.kraemer@uni-koeln.de.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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