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Originally published In Press as doi:10.1074/jbc.M210715200 on January 31, 2003

J. Biol. Chem., Vol. 278, Issue 15, 12820-12825, April 11, 2003
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Localization and Function of the Yeast Multidrug Transporter Tpo1p*

Markus Albertsen, Inga Bellahn, Reinhard Krämer, and Sabine WaffenschmidtDagger

From the Institut für Biochemie, Universität zu Köln, Zülpicher Strasse 47, 50674 Köln, Germany

In Saccharomyces cerevisiae four transporters, Tpo1p-Tpo4p, all members of the major facilitator superfamily, have been shown to confer resistance to polyamines. It was suggested that they act by pumping their respective substrate into the lumen of the vacuole depending on the proton gradient generated by the V-ATPase. Using sucrose gradient ultracentrifugation we found that an hemagglutinin (HA)-tagged Tpo1p as well as its HA-tagged Tpo2p-4p homologues co-localize with plasma membrane markers. Because the HA-tagged Tpo1p carrier protein proved to be functional in conferring resistance to polyamines in TPO1 knockouts, a function of Tpo1p in transport of polyamines across the plasma membrane seemed to be likely. The polyamine transport activity of wild type cells was compared with the respective activity of a TPO1 knockout strain. The results obtained strongly suggest that Tpo1p is a plasma membrane-bound exporter, involved in the detoxification of excess spermidine in yeast. When studying polyamine transport of wild type cells, we furthermore found that S. cerevisiae is excreting putrescine during the fermentative growth phase.

* This work was supported by Deutsche Forschungsgemeinschaft Grant GK 306 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.

Dagger To whom correspondence should be addressed. Tel.: 49-221-470-6426; Fax: 49-221-470-5091; E-mail waff@uni-koeln.de.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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