Eukaryotic Cell
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Eukaryotic Cell, October 2002, p. 799-810, Vol. 1, No. 5
1535-9778/02/$04.00+0     DOI: 10.1128/EC.1.5.799-810.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Dtr1p, a Multidrug Resistance Transporter of the Major Facilitator Superfamily, Plays an Essential Role in Spore Wall Maturation in Saccharomyces cerevisiae

Thomas Felder,1 Edith Bogengruber,1 Sandra Tenreiro,2 Adi Ellinger,3 Isabel Sá-Correia,2 and Peter Briza1*

Institut für Genetik und Allgemeine Biologie, Universität Salzburg, A-5020 Salzburg,1 Institut für Histologie und Embryologie, Universität Wien, A-1090 Vienna, Austria,3 Centro de Engenharia Biológica e Química, Instituto Superior Técnico, 1041-001 Lisbon, Portugal2

Received 19 April 2002/ Accepted 2 July 2002

The de novo formation of multilayered spore walls inside a diploid mother cell is a major landmark of sporulation in the yeast Saccharomyces cerevisiae. Synthesis of the dityrosine-rich outer spore wall takes place toward the end of this process. Bisformyl dityrosine, the major building block of the spore surface, is synthesized in a multistep process in the cytoplasm of the prospores, transported to the maturing wall, and polymerized into a highly cross-linked macromolecule on the spore surface. Here we present evidence that the sporulation-specific protein Dtr1p (encoded by YBR180w) plays an important role in spore wall synthesis by facilitating the translocation of bisformyl dityrosine through the prospore membrane. DTR1 was identified in a genome-wide screen for spore wall mutants. The null mutant accumulates unusually large amounts of bisformyl dityrosine in the cytoplasm and fails to efficiently incorporate this precursor into the spore surface. As a result, many mutant spores have aberrant surface structures. Dtr1p, a member of the poorly characterized DHA12 (drug:H+ antiporter with 12 predicted membrane spans) family, is localized in the prospore membrane throughout spore maturation. Transport by Dtr1p may not be restricted to its natural substrate, bisformyl dityrosine. When expressed in vegetative cells, Dtr1p renders these cells slightly more resistant against unrelated toxic compounds, such as antimalarial drugs and food-grade organic acid preservatives. Dtr1p is the first multidrug resistance protein of the major facilitator superfamily with an assigned physiological role in the yeast cell.

* Corresponding author. Mailing address: Institut für Genetik und Allgemeine Biologie, Universität Salzburg, Hellbrunnerstrasse 34, A-5020 Salzburg, Austria. Phone: (43) 662-8044-5769. Fax: (43) 662-8044-144. E-mail: peter.briza{at}sbg.ac.at.

Eukaryotic Cell, October 2002, p. 799-810, Vol. 1, No. 5
1535-9778/02/$04.00+0     DOI: 10.1128/EC.1.5.799-810.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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Copyright © 2002 by the American Society for Microbiology.