Overproduction of PDR3 Suppresses Mitochondrial Import Defects Associated with a TOM70 Null Mutation by Increasing the Expression of TOM72 in Saccharomyces cerevisiae

REFERENCES

• Abe, Y., T. Shodai, T. Muto, K. Mihara, H. Torii, S. Nishikawa, T. Endo, and D. Kohda. 2000. Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20. Cell 100:551–560.
   PubMed Web of Science ®Google Scholar
• Ahting, U., C. Thun, R. Hegerl, D. Typke, F. E. Nargang, W. Neupert, and S. Nussberger. 1999. The TOM core complex: the general protein import pore of the outer membrane of mitochondria. J. Cell Biol. 147:959–968.
   PubMed Web of Science ®Google Scholar
• Alam, R., N. Hachiya, M. Sakaguchi, S. Kawabata, S. Iwanaga, M. Kitajima, K. Mihara, and T. Omura. 1994. cDNA cloning and characterization of mitochondrial import stimulation factor (MSF) purified from rat liver cytosol. J. Biochem. (Tokyo) 116:416–425.
   PubMedGoogle Scholar
• Alconada, A., M. Kubrich, M. Moczko, A. Honlinger, and N. Pfanner. 1995. The mitochondrial receptor complex: the small subunit Mom8b/Isp6 supports association of receptors with the general insertion pore and transfer of preproteins. Mol. Cell. Biol. 15:6196–6205.
   PubMedGoogle Scholar
• Bedwell, D. M., D. J. Klionsky, and S. D. Emr. 1987. The yeast F1-ATPase beta subunit precursor contains functionally redundant mitochondrial protein import information. Mol. Cell. Biol. 7:4038–4047.
   PubMedGoogle Scholar
• Bedwell, D. M., S. A. Strobel, K. Yun, G. D. Jongeward, and S. D. Emr. 1989. Sequence and structural requirements of a mitochondrial protein import signal defined by saturation cassette mutagenesis. Mol. Cell. Biol. 9:1014–1025.
   PubMedGoogle Scholar
• Bolliger, L., T. Junne, G. Schatz, and T. Lithgow. 1995. Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria. EMBO J. 14:6318–6326.
   PubMedGoogle Scholar
• Bradford, M. M.. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248–254.
   PubMed Web of Science ®Google Scholar
• Brix, J., K. Dietmeier, and N. Pfanner. 1997. Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70. J. Biol. Chem. 272:20730–20735.
   PubMedGoogle Scholar
• Brix, J., S. Rudiger, B. Bukau, J. Schneider-Mergener, and N. Pfanner. 1999. Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein. J. Biol. Chem. 274:16522–16530.
   PubMedGoogle Scholar
• Caplan, A. J., D. M. Cyr, and M. G. Douglas. 1992. YDJ1.p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71:1143–1155.
   PubMed Web of Science ®Google Scholar
• Delaveau, T., A. Delahodde, E. Carvajal, J. Subik, and C. Jacq. 1994. PDR3, a new yeast regulatory gene, is homologous to PDR1 and controls the multidrug resistance phenomenon. Mol. Gen. Genet. 244:501–511.
   PubMedGoogle Scholar
• DeRisi, J., B. van den Hazel, P. Marc, E. Balzi, P. Brown, C. Jacq, and A. Goffeau. 2000. Genome microarray analysis of transcriptional activation in multidrug resistance yeast mutants. FEBS Lett. 470:156–160.
   PubMed Web of Science ®Google Scholar
• Emr, S. D., A. Vassarotti, J. Garrett, B. L. Geller, M. Takeda, and M. G. Douglas. 1986. The amino terminus of the yeast F1-ATPase beta-subunit precursor functions as a mitochondrial import signal. J. Cell Biol. 102:523–533.
   PubMedGoogle Scholar
• Gasser, S. M., A. Ohashi, G. Daum, P. C. Bohni, J. Gibson, G. A. Reid, T. Yonetani, and G. Schatz. 1982. Imported mitochondrial proteins cytochrome b2 and cytochrome c1 are processed in two steps. Proc. Natl. Acad. Sci. USA 79:267–271.
   PubMed Web of Science ®Google Scholar
• Gietz, R. D., and A. Sugino. 1988. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74:527–534.
   PubMed Web of Science ®Google Scholar
• Glaser, S. M., and M. G. Cumsky. 1990. A synthetic presequence reversibly inhibits protein import into yeast mitochondria. J. Biol. Chem. 265:8808–8816.
   PubMedGoogle Scholar
• Gratzer, S., T. Lithgow, R. E. Bauer, E. Lamping, F. Paltauf, S. D. Kohlwein, V. Haucke, T. Junne, G. Schatz, and M. Horst. 1995. Mas37p, a novel receptor subunit for protein import into mitochondria. J. Cell Biol. 129:25–34.
   PubMedGoogle Scholar
• Hachiya, N., T. Komiya, R. Alam, J. Iwahashi, M. Sakaguchi, T. Omura, and K. Mihara. 1994. MSF, a novel cytoplasmic chaperone which functions in precursor targeting to mitochondria. EMBO J. 13:5146–5154.
   PubMedGoogle Scholar
• Hajek, P., and D. M. Bedwell. 1994. Characterization of the mitochondrial binding and import properties of purified yeast F1-ATPase beta subunit precursor. Import requires external ATP. J. Biol. Chem. 269:7192–7200.
   PubMedGoogle Scholar
• Hajek, P., J. Y. Koh, L. Jones, and D. M. Bedwell. 1997. The amino terminus of the F1-ATPase beta-subunit precursor functions as an intramolecular chaperone to facilitate mitochondrial protein import. Mol. Cell. Biol. 17:7169–7177.
   PubMedGoogle Scholar
• Hallstrom, T. C., and W. S. Moye-Rowley. 2000. Multiple signals from dysfunctional mitochondria activate the pleiotropic drug resistance pathway in Saccharomyces cerevisiae. J. Biol. Chem. 275:37347–37356.
   PubMed Web of Science ®Google Scholar
• Haucke, V., T. Lithgow, S. Rospert, K. Hahne, and G. Schatz. 1995. The yeast mitochondrial protein import receptor Mas20p binds precursor proteins through electrostatic interaction with the positively charged presequence. J. Biol. Chem. 270:5565–5570.
   PubMed Web of Science ®Google Scholar
• Hines, V., A. Brandt, G. Griffiths, H. Horstmann, H. Brutsch, and G. Schatz. 1990. Protein import into yeast mitochondria is accelerated by the outer membrane protein MAS70. EMBO J. 9:3191–3200.
   PubMed Web of Science ®Google Scholar
• Hines, V., and G. Schatz. 1993. Precursor binding to yeast mitochondria. A general role for the outer membrane protein Mas70p. J. Biol. Chem. 268:449–454.
   PubMedGoogle Scholar
• Honlinger, A., U. Bomer, A. Alconada, C. Eckerskorn, F. Lottspeich, K. Dietmeier, and N. Pfanner. 1996. Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein import. EMBO J. 15:2125–2137.
   PubMedGoogle Scholar
• Hönlinger, A., M. Kübrich, M. Moczko, F. Gärtner, L. Mallet, F. Bussereau, C. Eckerskorn, F. Lottspeich, K. Dietmeier, M. Jacquet, and N. Pfanner. 1995. The mitochondrial receptor complex: Mom22 is essential for cell viability and directly interacts with preproteins. Mol. Cell. Biol. 15:3382–3389.
   PubMedGoogle Scholar
• Horwich, A. L., F. Kalousek, I. Mellman, and L. E. Rosenberg. 1985. A leader peptide is sufficient to direct mitochondrial import of a chimeric protein. EMBO J. 4:1129–1135.
   PubMedGoogle Scholar
• Hurt, E. C., D. S. Allison, U. Muller, and G. Schatz. 1987. Amino-terminal deletions in the presequence of an imported mitochondrial protein block the targeting function and proteolytic cleavage of the presequence at the carboxy terminus. J. Biol. Chem. 262:1420–1424.
   PubMedGoogle Scholar
• Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163–168.
   PubMed Web of Science ®Google Scholar
• Jia, Y., B. Rothermel, J. Thornton, and R. A. Butow. 1997. A basic helix-loop-helix–leucine zipper transcription complex in yeast functions in a signaling pathway from mitochondria to the nucleus. Mol. Cell. Biol. 17:1110–1117.
   PubMed Web of Science ®Google Scholar
• Johnston, M., S. Andrews, R. Brinkman, J. Cooper, H. Ding, J. Dover, Z. Du, A. Favello, L. Fulton, S. Gattung, et al.. 1994. Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII. Science 265:2077–2082.
   PubMedGoogle Scholar
• Kassenbrock, C. K., W. Cao, and M. G. Douglas. 1993. Genetic and biochemical characterization of ISP6, a small mitochondrial outer membrane protein associated with the protein translocation complex. EMBO J. 12:3023–3034.
   PubMedGoogle Scholar
• Kean, L. S., A. M. Grant, C. Angeletti, Y. Mahe, K. Kuchler, R. S. Fuller, and J. W. Nichols. 1997. Plasma membrane translocation of fluorescent-labeled phosphatidylethanolamine is controlled by transcription regulators, PDR1 and PDR3. J. Cell Biol. 138:255–270.
   PubMedGoogle Scholar
• Kronidou, N. G., W. Oppliger, L. Bolliger, K. Hannavy, B. S. Glick, G. Schatz, and M. Horst. 1994. Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane. Proc. Natl. Acad. Sci. USA 91:12818–12822.
   PubMedGoogle Scholar
• Liao, X., and R. A. Butow. 1993. RTG1 and RTG2: two yeast genes required for a novel path of communication from mitochondria to the nucleus. Cell 72:61–71.
   PubMed Web of Science ®Google Scholar
• Lithgow, T., B. S. Glick, and G. Schatz. 1995. The protein import receptor of mitochondria. Trends Biochem. Sci. 20:98–101.
   PubMed Web of Science ®Google Scholar
• Lithgow, T., T. Junne, K. Suda, S. Gratzer, and G. Schatz. 1994. The mitochondrial outer membrane protein Mas22p is essential for protein import and viability of yeast. Proc. Natl. Acad. Sci. USA 91:11973–11977.
   PubMedGoogle Scholar
• Lithgow, T., T. Junne, C. Wachter, and G. Schatz. 1994. Yeast mitochondria lacking the two import receptors Mas20p and Mas70p can efficiently and specifically import precursor proteins. J. Biol. Chem. 269:15325–15330.
   PubMedGoogle Scholar
• Maccecchini, M. L., Y. Rudin, G. Blobel, and G. Schatz. 1979. Import of proteins into mitochondria: precursor forms of the extramitochondrially made F1-ATPase subunits in yeast. Proc. Natl. Acad. Sci. USA 76:343–347.
   PubMed Web of Science ®Google Scholar
• Martin, J., K. Mahlke, and N. Pfanner. 1991. Role of an energized inner membrane in mitochondrial protein import. Delta psi drives the movement of presequences. J. Biol. Chem. 266:18051–18057.
   PubMedGoogle Scholar
• Murakami, H., D. Pain, and G. Blobel. 1988. 70-kD heat shock-related protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondria. J. Cell Biol. 107:2051–2057.
   PubMedGoogle Scholar
• Nourani, A., M. Wesolowski-Louvel, T. Delaveau, C. Jacq, and A. Delahodde. 1997. Multiple-drug-resistance phenomenon in the yeast Saccharomyces cerevisiae: involvement of two hexose transporters. Mol. Cell. Biol. 17:5453–5460.
   PubMedGoogle Scholar
• Pullman, M. E., H. S. Penefsky, A. Datta, and E. Racker. 1960. Partial resolution of the enzymes catalyzing oxidative phosphorylation. I. Purification and properties of soluble, dinitrophenyl-stimulated adenosine triphosphatase. J. Biol. Chem. 235:3322–3329.
   PubMed Web of Science ®Google Scholar
• Ramage, L., T. Junne, K. Hahne, T. Lithgow, and G. Schatz. 1993. Functional cooperation of mitochondrial protein import receptors in yeast. EMBO J. 12:4115–4123.
   PubMed Web of Science ®Google Scholar
• Rassow, J., A. C. Maarse, E. Krainer, M. Kubrich, H. Muller, M. Meijer, E. A. Craig, and N. Pfanner. 1994. Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44. J. Cell Biol. 127:1547–1556.
   PubMed Web of Science ®Google Scholar
• Roise, D., and G. Schatz. 1988. Mitochondrial presequences. J. Biol. Chem. 263:4509–4511.
   PubMed Web of Science ®Google Scholar
• Roise, D., F. Theiler, S. J. Horvath, J. M. Tomich, J. H. Richards, D. S. Allison, and G. Schatz. 1988. Amphiphilicity is essential for mitochondrial presequence function. EMBO J. 7:649–653.
   PubMedGoogle Scholar
• Rose, M. D., F. Winston, and P. Heiter. 1990. Methods in yeast genetics: a laboratory course manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y
   Google Scholar
• Schiestl, R. H., and R. D. Gietz. 1989. High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr. Genet. 16:339–346.
   PubMed Web of Science ®Google Scholar
• Schlossmann, J., R. Lill, W. Neupert, and D. A. Court. 1996. Tom71, a novel homologue of the mitochondrial preprotein receptor Tom70. J. Biol. Chem. 271:17890–17895.
   PubMedGoogle Scholar
• Schmitt, M. E., T. A. Brown, and B. L. Trumpower. 1990. A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae. Nucleic Acids Res. 18:3091–3092.
   PubMed Web of Science ®Google Scholar
• Schneider, H. C., J. Berthold, M. F. Bauer, K. Dietmeier, B. Guiard, M. Brunner, and W. Neupert. 1994. Mitochondrial Hsp70/MIM44 complex facilitates protein import. Nature 371:768–774.
   PubMed Web of Science ®Google Scholar
• Sherman, F., G. R. Fink, and L. W. Lawrence. 1979. Methods in yeast genetics: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y
   Google Scholar
• Ungermann, C., B. Guiard, W. Neupert, and D. M. Cyr. 1996. The delta psi- and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria. EMBO J. 15:735–744.
   PubMedGoogle Scholar
• Vassarotti, A., W. J. Chen, C. Smagula, and M. G. Douglas. 1987. Sequences distal to the mitochondrial targeting sequences are necessary for the maturation of the F1-ATPase β-subunit precursor in mitochondria. J. Biol. Chem. 262:411–418.
   PubMedGoogle Scholar
• Vestweber, D., and G. Schatz. 1988. Point mutations destabilizing a precursor protein enhance its post-translational import into mitochondria. EMBO J. 7:1147–1151.
   PubMedGoogle Scholar
• von Heijne, G.. 1986. Mitochondrial targeting sequences may form amphiphilic helices. EMBO J. 5:1335–1342.
   PubMed Web of Science ®Google Scholar