The preprotein translocase of the mitochondrial outer membrane

Biological Chemistry

Volumn 379, Issue 3, 1998, Pages 289-294

  Ryan, Michael T ^a   Pfanner, Nikolaus ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

Author keywords

Biogenesis; Mitochondria; Protein import; Receptor; Tom

Indexed keywords

CARRIER PROTEIN; MEMBRANE RECEPTOR; MITOCHONDRIAL ENZYME; OUTER MEMBRANE PROTEIN; PROTEIN PRECURSOR;

ARTICLE; MITOCHONDRIAL MEMBRANE; MITOCHONDRION; PRIORITY JOURNAL; PROTEIN TRANSPORT;

ADENOSINE TRIPHOSPHATASES; BACTERIAL PROTEINS; BIOLOGICAL TRANSPORT; CYTOSOL; ESCHERICHIA COLI PROTEINS; INTRACELLULAR MEMBRANES; MEMBRANE TRANSPORT PROTEINS; MITOCHONDRIA; RECEPTORS, CYTOPLASMIC AND NUCLEAR;

EID: 0031900451     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (35)

1. Alconada, A., Kübrich, M., Moczco, M., Hönlinger, A., and Pfanner, N. (1995). The mitochondrial receptor complex: the small subunit Mom8b/lsp6 supports association of receptors with the general insertion pore and transfer of preproteins. Mol. Cell. Biol. 15, 6196-6205.
2. Baker, K.P., Schaniel, A., Vestweber, D., and Schatz, G. (1990). A yeast mitochondrial outer membrane protein essential for protein import and cell viability. Nature 348, 605-609.
3. Bolliger, L., Junne, T., Schatz, G., and Lithgow, T. (1995). Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria. EMBO J. 14, 6318-6326.
4. Brix, J., Dietmeier, K., and Pfanner, N. (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.
5. Court, D.A., Nargang, F.E., Steiner, H., Hodges, R.S., Neupert, W., and Lill, R. (1996). Role of the intermembrane-space domain of the preprotein receptor Tom22 in protein import into mitochondria. Mol. Cell. Biol. 16, 4035-4042.
6. Dekker, P.J.T., Martin, F., Maarse, A.C., Bömer, U., Müller, H., Guiard, B., Meijer, M., Rassow, J., and Pfanner, N. (1997). The tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44. EMBO J. 16, 5408-5419.
7. Dietmeier, K., Hönlinger, A., Bömer, U., Dekker, P.J.T., Eckerskorn, C., Lottspeich F., Kübrich, M., and Pfanner, N. (1997). Tom5 functionally links mitochondrial preprotein receptors to the general import pore. Nature 388, 195-200.
8. Gratzer, S., Lithgow, T., Bauer, R.E., Lamping, E., Paltauf, F., Kohlwein, S.D., Haucke, V., Junne, T., Schatz, G., and Horst, M. (1995). Mas37p, a novel receptor subunit for protein import into mitochondria. J. Cell Biol. 129, 25-34.
9. Hachiya, N., Mihara, K., Suda, K., Horst, M., Schatz, G., and Lithgow, T. (1995). Reconstitution of the initial steps of mitochondrial protein import. Nature 376, 705-709.
10. Harkness, T.A., Nargang, F.E., van der Klei, I., Neupert, W., and Lill, R. (1994). A crucial role of the mitochondrial protein import receptor MOM19 for the biogenesis of mitochondria. J. Cell. Biol. 124, 637-648.
11. Haucke, V., Horst, M., Schatz, G., and Lithgow, T. (1996). The Mas20p and Mas70p subunits of the protein import receptor of yeast mitochondria interact via the tetratricopeptide repeat motif in Mas20p: evidence for a single hetero-oligomeric receptor. EMBO J. 15, 1231-1237.
12. Hönlinger, A., Kübrich, M., Moczko, M., Gärtner, F., Mallet, L., Bussereau, F., Eckerskorn, C., Lottspeich, F., Dietmeier, K., Jacquet, M., and Pfanner, N. (1995). The mitochondrial receptor complex: Mom22 is essential for cell viability and directly interacts with preproteins. Mol. Cell Biol. 15, 3382-3389.
13. Hönlinger, A, Bömer, U., Alconada, A., Eckerskorn, C., Lottspeich, F., Dietmeier, K., and Pfanner, N. (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.
14. Kassenbrock, C.K., Cao, W., and Douglas, M.G. (1993). Genetic and biochemical characterization of ISP6, a small mitochondrial outer membrane protein associated with the protein translocation complex. EMBO J. 8, 3023-3034.
15. Kiebler, M., Pfaller, R., Söllner, T., Griffiths, G., Horstman, H., Pfanner, N., and Neupert, W. (1990). Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins. Nature 348, 610-616.
16. Kiebler, M., Keil, P., Schneider, H., van der Klei, I.J., Pfanner, N., and Neupert, W. (1993). The mitochondrial receptor complex: a central role of MOM22 in mediating preprotein transfer from receptors to the general insertion pore. Cell 74, 483-492.
17. Keil, P., and Pfanner, N. (1993). Insertion of MOM22 into the mitochondrial outer membrane strictly depends on surface receptors. FEBS Lett. 321, 197-200.
18. Keil, P., Weinzierl, A., Kiebler, M., Dietmeier, K., Söllner, T., and Pfanner, N. (1993). Biogenesis of the mitochondrial receptor complex. Two receptors are required for binding of MOM38 to the outer membrane surface. J. Biol. Chem. 268, 19177-19180.
19. Lithgow, T., Junne, T., Suda, K., Gratzer, S., and Schatz, G. (1994). The mitochondrial outer membrane protein Mas22p is essential for protein import and viability of yeast. Proc. Natl. Acad. Sci. USA 91, 11973-11977.
20. Manella, C.A., Neuwald, A.F., and Lawrence, C.E. (1996). Detection of likely transmembrane β-strand regions in sequences of mitochondrial pore proteins using the Gibbs sampler. J. Bioenerg. Biomem. 28, 163-169.
21. Mayer, A., Nargang, F.E., Neupert, W., and Lill, R. (1995a) MOM22 is a receptor for mitochondrial targeting sequences and cooperates with MOM19. EMBO J. 14, 4204-4211.
22. Mayer, A., Neupert, W., and Lill, R. (1995b). 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.
23. Moczko, M., Gärtner, F., and Pfanner, N. (1993). The protein import receptor MOM19 of yeast mitochondria. FEBS Lett. 326, 251-254.
24. Moczko, M., Bömer, U., Kübrich, M., Zufall, N., Hönlinger, A., and Pfanner, N. (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.
25. Nakai, M., Kinoshita, K., and Endo, T. (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.
26. Pfaller, R., Pfanner, N., and Neupert, W. (1989). Mitochondrial protein import. Bypass of proteinaceous surface receptors can occur with low specificity and efficiency. J. Biol. Chem. 264, 34-39.
27. Pfanner, N., and Meijer, M. (1995). Protein sorting: Pulling in the proteins. Current Biol. 5, 132-135.
28. Ramage, L., Junne, T., Hahne, K., Lithgow, T., and Schatz, G. (1993). Functional cooperation of mitochondrial protein import receptors in yeast. EMBO J. 12, 4115-4123.
29. Rapaport, D., Neupert, W., and Lill, R. (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.
30. Schatz, G. (1997). Just follow the acid chain. Nature 388, 121-122.
31. Schlossmann, J., Dietmeier, K., Pfanner, N., and Neupert, W. (1994). Specific recognition of mitochondrial preproteins by the cytosolic domain of the import receptor MOM72. J. Biol. Chem. 269, 11893-11901.
32. Schneider, H., Söllner, T., Dietmeier, K., Eckerskorn, C., Lottspeich, F., Trülzsch, B., Neupert, W., and Pfanner, N. (1991). Targeting of the master receptor MOM19 to mitochondria. Science 254, 1659-1662.
33. Söllner, T., Griffiths, G., Pfaller, R., Pfanner, N., and Neupert, W. (1989). MOM19, an import receptor for mitochondrial precursor proteins. Cell 254, 1061-1070.
34. Vestweber, D., Brunner, J., Baker, A., and Schatz, G. (1989). A 42K outer-membrane protein is a component of the yeast mitochondrial protein import site. Nature 341, 205-209.
35. von Heijne, G. (1986). Mitochondrial targeting sequences form amphiphilic helices. EMBO J. 5, 1335-1342.