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Cell and Organelle Structure and Assembly

Role of the Negative Charges in the Cytosolic Domain of TOM22 in the Import of Precursor Proteins into Mitochondria

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Pages 3173-3181 | Received 18 Nov 1997, Accepted 17 Mar 1998, Published online: 28 Mar 2023

REFERENCES

  • Akins, R. A., and A. M. Lambowitz 1985. General method for cloning Neurospora crassa nuclear genes by complementation of mutants. Mol. Cell. Biol. 5: 2272–2278.
  • Austin, B., R. M. Hall, and B. M. Tyler 1990. Optimized vectors for transformation of Neurospora crassa and Aspergillus nidulans to bleomycin and phleomycin resistance. Gene 93: 157–162.
  • Ausubel, R. A., R. Brent, R. E. Kingston, D. D. Moore, and J. G. Seidman 1992. Current protocols in molecular biology. Greene and Wiley Interscience, New York, N.Y.
  • Bauer, M. F., C. Sirrenberg, W. Neupert, and M. Brunner 1996. Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria. Cell 87: 33–41.
  • Bernstein, H. D., M. A. Poritz, K. Strub, P. J. Hoben, S. Brenner, and P. Walter 1989. Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle. Nature 340: 482–486.
  • 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.
  • Bradford, M. M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72: 248–254.
  • 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.
  • Cartwright, P., T. Beilharz, P. Hansen, J. Garrett, and T. Lithgow 1997. Mft52, and acid-bristle protein in the cytosol that delivers precursor proteins to yeast mitochondria. J. Biol. Chem. 272: 5320–5325.
  • Court, D. A., F. E. Nargang, H. Steiner, R. S. Hodges, W. Neupert, and R. Lill 1996. Role of the intermembrane space domain of the preprotein receptor Tom22 in protein import into mitochondria. Mol. Cell. Biol. 16: 4034–4042.
  • Davis, R. H., and F. J. De Serres 1970. Genetic and microbiological research techniques for Neurospora crassa. Methods Enzymol. 17: 79–143.
  • Dietmeier, K., A. Hönlinger, U. Bömer, P. J. T. Dekker, C. Eckerskorn, F. Lottspeich, M. Kübrich, and N. Pfanner 1997. Tom5 functionally links mitochondrial preprotein receptors to the general import pore. Nature 388: 195–200.
  • Drygas, M. E., A. M. Lambowitz, and F. E. Nargang 1989. Cloning and analysis of the Neurospora crassa gene for cytochrome c heme lyase. J. Biol. Chem. 264: 17897–17907.
  • Good, A. G., and W. L. Crosby 1989. Anaerobic induction of alanine aminotransferase in barley root tissue. Plant Physiol. 90: 1305–1309.
  • 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.
  • Harkness, T. A. A., F. E. Nargang, I. Van der Klei, W. Neupert, and R. Lill 1994. A crucial role of the mitochondrial protein import receptor MOM19 for the biogenesis of mitochondria. J. Cell Biol. 124: 637–648.
  • 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.
  • 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.
  • 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.
  • Hurt, E. C., B. Pesold-Hurt, and G. Schatz 1984. The cleavable prepiece of an imported mitochondrial protein is sufficient to direct cytosolic dihydrofolate reductase into the mitochondrial matrix. FEBS Lett. 178: 306–310.
  • Hurt, E. C., B. Pesold-Hurt, K. Suda, W. Oppliger, and G. Schatz 1985. The first twelve amino acids (less than half of the presequence) can direct mouse cytosolic dihydrofolate reductase into the yeast mitochondrial matrix. EMBO J. 4: 2061–2068.
  • Iwahashi, J., S. Yamazaki, T. Komiya, N. Nomura, S. Nishikawa, T. Endo, and K. Mihara 1997. Analysis of the functional domain of the rat liver mitochondrial import receptor Tom20. J. Biol. Chem. 272: 18467–18472.
  • Kerscher, O., J. Holder, M. Srinivasan, R. S. Leung, and R. E. Jensen 1997. The Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane. J. Cell Biol. 139: 1663–1675.
  • Kiebler, M., P. Keil, H. Schneider, I. van der Klei, N. Pfanner, and W. Neupert 1993. The mitochondrial receptor complex: a central role of MOM22 in mediating transfer of preproteins from receptors to the general insertion pore. Cell 74: 483–492.
  • Koehler, C. M., E. Jarosch, K. Tokatlidis, D. Schmid, R. J. Schweyen, and G. Schatz 1998. Import of mitochondrial carriers mediated by essential proteins of the intermembrane space. Science 279: 369–373.
  • Komiya, T., S. Rospert, G. Schatz, and K. Mihara 1997. Binding of mitochondrial precursor proteins to the cytoplasmic domains of the import receptors Tom70 and Tom20 is determined by cytoplasmic chaperones. EMBO J. 16: 4267–4275.
  • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.
  • Lill, R., and W. Neupert 1996. Mechanisms of protein import across the mitochondrial outer membrane. Trends Cell Biol. 6: 56–61.
  • 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.
  • Martin, J., K. Mahlke, and N. Pfanner 1991. Role of an energized inner membrane in mitochondrial protein import. J. Biol. Chem. 266: 18051–18057.
  • Mayer, A., R. Lill, and W. Neupert 1993. Translocation and insertion of precursor proteins into isolated outer membranes of mitochondria. J. Cell Biol. 121: 1233–1243.
  • Mayer, A., F. E. Nargang, W. Neupert, and R. Lill 1995. MOM22 is a receptor for mitochondrial targeting sequences and cooperates with MOM19. EMBO J. 14: 4204–4211.
  • Mayer, A., W. Neupert, and R. Lill 1995. Mitochondrial protein import: Reversible binding of the presequence at the trans side of the outer membrane drives partial translocation and unfolding. Cell 80: 127–137.
  • Moczko, M., U. Bömer, M. Kübrich, N. Zufall, A. Hönlinger, and N. Pfanner 1997. The intermembrane space domain of mitochondrial Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences. Mol. Cell. Biol. 17: 6574–6584.
  • Moczko, M., B. Ehmann, F. Gärtner, A. Hönlinger, E. Schäfer, and N. Pfanner 1994. Deletion of the receptor MOM19 strongly impairs import of cleavable preproteins into Saccharomyces cerevisiae mitochondria. J. Biol. Chem. 269: 9045–9051.
  • Nakai, M., and T. Endo 1995. Identification of yeast MAS17 encoding the functional counterpart of the mitochondrial receptor complex protein MOM22 of Neurospora crassa. FEBS Lett. 357: 202–206.
  • Nakai, M., K. Kinoshita, and T. Endo 1995. Mitochondrial receptor complex protein. The intermembrane space domain of yeast Mas17 is not essential for its targeting or function. J. Biol. Chem. 270: 30571–30575.
  • Nargang, F. E. Unpublished data.
  • Nargang, F. E., M. E. Drygas, P. L. Kwong, D. W. Nicholson, and W. Neupert 1988. A mutant of Neurospora crassa deficient in cytochrome c heme lyase activity cannot import cytochrome c into mitochondria. J. Biol. Chem. 263: 9388–9394.
  • Nargang, F. E., K.-P. Künkele, A. Mayer, R. G. Ritzel, W. Neupert, and R. Lill 1995. “Sheltered disruption” of Neurospora crassa MOM22, an essential component of the mitochondrial protein import complex. EMBO J. 14: 1099–1108.
  • Nargang, F. E., and R. Lill 1996. Import of proteins into mitochondria The Mycota III. In: Brambl, R., and G. Marzluf85–107Springer-Verlag, Berlin, Germany.
  • Neupert, W. 1997. Protein import into mitochondria. Annu. Rev. Biochem. 66: 863–917.
  • Pfaller, R., N. Pfanner, and W. Neupert 1989. Mitochondrial protein import: bypass of proteinaceous surface receptors can occur with low specificity and efficiency. J. Biol. Chem. 264: 34–39.
  • Pfanner, N., E. A. Craig, and A. Hönlinger 1997. Mitochondrial preprotein translocase. Annu. Rev. Cell Dev. Biol. 13: 25–51.
  • Pfanner, N., and W. Neupert 1990. The mitochondrial protein import apparatus. Annu. Rev. Biochem. 59: 331–353.
  • Pfanner, N., and W. Neupert 1985. Transport of proteins into mitochondria: a potassium diffusion potential is able to drive the import of ADP/ATP carrier. EMBO J. 4: 2819–2825.
  • Pfanner, N., M. Tropschug, and W. Neupert 1987. Mitochondrial protein import: nucleoside triphosphates are involved in conferring import-competence to precursors. Cell 49: 815–823.
  • Rapaport, D., K.-P. Künkele, M. Dembowski, U. Ahting, F. E. Nargang, W. Neupert, and R. Lill. Dynamics of the TOM complex of mitochondria during binding and translocation of preproteins. Submitted for publication.
  • Rapaport, D., A. Mayer, W. Neupert, and R. Lill 1998. cis and trans sites of the TOM complex of mitochondria in unfolding and initial translocation of preproteins. J. Biol. Chem. 273: 8806–8813.
  • Rapaport, D., W. Neupert, and R. Lill 1997. Mitochondrial protein import: Tom40 plays a major role in targeting and translocation of preproteins by forming a specific binding site for the presequence. J. Biol. Chem. 272: 18725–18731.
  • Rodriguez-Cousino, N., F. E. Nargang, R. Baardman, W. Neupert, R. Lill, and D. A. Court. An import signal in the cytosolic domain of the Neurospora mitochondrial outer membrane protein TOM22. J. Biol. Chem., in press.
  • Roise, D., and G. Schatz 1988. Mitochondrial presequences. J. Biol. Chem. 263: 4509–4511.
  • Ryan, K. R., and R. E. Jensen 1995. Protein translocation across mitochondrial membranes: What a long, strange trip it is. Cell 83: 517–519.
  • Ryan, K. R., R. S. Leung, and R. E. Jensen 1998. Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not other Tim23p molecules. Mol. Cell. Biol. 18: 178–187.
  • Schatz, G. 1997. Just follow the acid chain. Nature 388: 121–122.
  • Schatz, G. 1996. The protein import system of mitochondria. J. Biol. Chem. 271: 31763–31766.
  • Schleiff, E., G. C. Shore, and I. S. Goping 1997. Interactions of the human mitochondrial protein import receptor hTOM20 with precursor proteins in vitro reveal pleiotropic specificities and different receptor domain requirements. J. Biol. Chem. 272: 17784–17789.
  • Schweizer, M., M. E. Case, C. C. Dykstra, N. H. Giles, and S. R. Kushner 1981. Identification and characterization of recombinant plasmids carrying the complete qa gene cluster from Neurospora crassa including the qa-1+ regulatory gene. Proc. Natl. Acad. Sci. USA 78: 5086–5090.
  • Sirrenberg, C., M. Bauer, B. Guiard, W. Neupert, and M. Brunner 1996. Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22. Nature 384: 582–585.
  • Sirrenberg, C., M. Endres, H. Fölsch, R. A. Stuart, W. Neupert, and M. Brunner 1998. Carrier protein import into mitochondria mediated by the intermembrane space proteins Tim10/Mrs11p and Tim12/Mrs10p. Nature 391: 912–915.
  • Vogelstein, B., and D. Gillespie 1979. Preparative and analytical purification of DNA from agarose. Proc. Natl. Acad. Sci. USA 73: 615–619.
  • von Heijne, G. 1986. Mitochondrial targeting sequences may form amphiphilic helices. EMBO J. 5: 1335–1342.
  • von Heijne, G. 1996. Targeting signals for protein import into mitochondria and other subcellular organelles. Adv. Mol. Cell Biol. 17: 1–12.
  • White, B., and D. Woodward 1995. A simple method for making disposable race tubes. Fungal Genet. Newsl. 42: 79.

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