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Originally published In Press as doi:10.1074/jbc.M106285200 on October 15, 2001

J. Biol. Chem., Vol. 276, Issue 51, 47844-47852, December 21, 2001
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Saccharomyces cerevisiae Multidrug Resistance Gene Expression Inversely Correlates with the Status of the F0 Component of the Mitochondrial ATPase*

Xiaoting ZhangDagger and W. Scott Moye-RowleyDagger §

From the § Department of Physiology and Biophysics and Dagger  Molecular Biology Ph.D. Program, University of Iowa, Iowa City, Iowa 52242

Loss of the mitochondrial genome (rho 0 cell) or elimination of the mitochondrial inner membrane protein Oxa1p causes a dramatic increase in expression of the ATP binding cassette transporter-encoding gene PDR5 in the yeast Saccharomyces cerevisiae. This increase in gene expression occurs via activation of the function of the Cys6-Zn(II)2 cluster transcription factor Pdr3p, which in turn autoregulates expression of its structural gene. Surprisingly, the acquisition of PDR5-dependent multidrug resistance occurs at a very high frequency, consistent with the appearance of rho - cells in a fermentatively growing culture (~2%). The degree of activation of Pdr3p target genes was found to vary considerably and to be influenced by the presence of the homologous protein, Pdr1p. Mutagenesis and overexpression studies provided evidence that the control of Pdr3p expression was the major control point of this transcription factor by mitochondrial retrograde signaling. Because both rho 0 and oxa1 mutant cells have multiple defects including loss of normal respiratory chain function and oxidative phosphorylation, a series of mutant strains with more selective defects in mitochondrial function was employed to identify the molecular signal that triggers PDR5 transcriptional activation. Only mutations that influenced the functional status of the F0 subunit of the mitochondrial ATPase were found to lead to activation of PDR5 expression.

* This work was supported by National Institutes of Health Grant GM49825 (to W. S. M.).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: Dept. of Physiology and Biophysics, 5-612 Bowen Science Bldg., University of Iowa, Iowa City, IA 52242. Tel.: 319-335-7874; Fax: 319-335-7330; E-mail: moyerowl@blue.weeg.uiowa.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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