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Journal of Bacteriology, September 2000, p. 5196-5201, Vol. 182, No. 18
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Cholate Resistance in Lactococcus lactis Is Mediated by an ATP-Dependent Multispecific Organic Anion Transporter

Atsushi Yokota,1 Marloes Veenstra,2 Peter Kurdi,3 Hendrik W. van Veen,2,* and Wil N. Konings2

Laboratory of Microbial Resources and Ecology1 and Laboratory of Applied Microbiology,3 Research Group of Molecular Bioscience, Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University, Sapporo 060-8589, Japan, and Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, NL-9750 AA Haren, The Netherlands2

Received 13 April 2000/Accepted 16 June 2000

The cholate-resistant Lactococcus lactis strain C41-2, derived from wild-type L. lactis MG1363 through selection for growth on cholate-containing medium, displayed a reduced accumulation of cholate due to an enhanced active efflux. However, L. lactis C41-2 was not cross resistant to deoxycholate or cationic drugs, such as ethidium and rhodamine 6G, which are typical substrates of the multidrug transporters LmrP and LmrA in L. lactis MG1363. The cholate efflux activity in L. lactis C41-2 was not affected by the presence of valinomycin plus nigericin, which dissipated the proton motive force. In contrast, cholate efflux in L. lactis C41-2 was inhibited by ortho-vanadate, an inhibitor of P-type ATPases and ATP-binding cassette transporters. Besides ATP-dependent drug extrusion by LmrA, two other ATP-dependent efflux activities have previously been detected in L. lactis, one for the artificial pH probe 2',7'-bis-(2-carboxyethyl)-5(and 6)-carboxyfluorescein (BCECF) and the other for the artificial pH probe N-(fluorescein thio-ureanyl)-glutamate (FTUG). Surprisingly, the efflux rate of BCECF, but not that of FTUG, was significantly enhanced in L. lactis C41-2. Further experiments with L. lactis C41-2 cells and inside out membrane vesicles revealed that cholate and BCECF inhibit the transport of each other. These data demonstrate the role of an ATP-dependent multispecific organic anion transporter in cholate resistance in L. lactis.

* Corresponding author. Mailing address: Department of Microbiology, Biological Center, University of Groningen, Kerklaan 30, P.O. Box 14, NL-9750 AA Haren, The Netherlands. Phone: 31-50-363-2150. Fax: 31-50-363-2154. E-mail: h.w.van.veen{at}biol.rug.nl.

Journal of Bacteriology, September 2000, p. 5196-5201, Vol. 182, No. 18
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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