Under conditions of insufficient permeability of VDAC1, external NADH may use the TOM complex channel to cross the outer membrane of Saccharomyces cerevisiae mitochondria

Journal of Bioenergetics and Biomembranes

Volumn 33, Issue 2, 2001, Pages 119-126

  Antos, Nina ^a   Stobienia, Olgierd ^a   Budzińska, Małgorzata ^a   Kmita, Hanna ^a  

^a INSTITUTE OF MOLECULAR PHYSICS   (Poland)

Author keywords

External NADH transport; Isoform1 of voltage dependent anion channel (VDAC1); Saccharomyces cerevisiae mitochondria; TOM complex channel

Indexed keywords

ANION CHANNEL; OUTER MEMBRANE PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; CHANNEL GATING; MEMBRANE PERMEABILITY; MITOCHONDRIAL MEMBRANE; NONHUMAN; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE;

INTRACELLULAR MEMBRANES; MEMBRANE TRANSPORT PROTEINS; MITOCHONDRIA; NAD; OXIDATION-REDUCTION; PERMEABILITY; PORINS; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TETRAHYDROFOLATE DEHYDROGENASE; VOLTAGE-DEPENDENT ANION CHANNEL 1; VOLTAGE-DEPENDENT ANION CHANNEL 2; VOLTAGE-DEPENDENT ANION CHANNELS;

EID: 0035007796     PISSN: 0145479X     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1010748431000     Document Type: Article

References (43)

1. Benz, R. (1994). Biochim. Biophys. Acta 1197, 167-196.
2. Benz, R., Janko, K., Boos, W., and Lauger, P. (1978). Biochim. Biophys. Acta 511, 305-319.
3. Blachly-Dyson, E., Zambrowicz, E. B., Yu., W. H., Adams, V., McCabe, E. R. B., Adelman, J., Colombini, M., and Forte, M. (1993). J. Biol. Chem. 268, 1835-1841.
4. Blachly-Dyson, E., Song, J., Wolfgang, W. J., Colombini, M., and Forte, M. (1997). Mol. Cell. Biol. 17, 5727-5738.
5. Colombini, M. (1979). Nature (London) 279, 643-645.
6. Colombini, M., Blachly-Dyson, E., and Forte, M. (1996). In Ion Channels: VDAC, A Channel in the Outer Mitochondrial Membrane (Narahashi, T., ed.), Plenum Press, New York, pp. 169-201.
7. Daum, G., Bohni, P. C., and Schatz, G. (1982). J. Biol. Chem. 257, 13028-13033.
8. Dekker, P. J., Martin, F., Maarse, A. C., Bümer, U., Müller, H., Guiard, B., Meijer, M., Rassow, J., and Pfanner, N. (1997). EMBO J. 16, 5408-5419.
9. De Pinto, V., Ludwig, O., Krause, J., Benz, R., and Palmieri, F. (1987). Biochim. Biophys. Acta 894, 109-119.
10. De Vries, S. and Marres, C. A. M. (1987). Biochim. Biophys. Acta 895, 205-239.
11. Dihanich, M., Suda, K., and Schatz, G. (1987). EMBO J. 6, 723-728.
12. Dihanich, M., Schmid, A., Oppliger, W., and Benz, R. (1989). Eur. J. Biochem. 181, 703-708.
13. Douce, R., Bourguignon, J., Brouquisse, R., and Neuberger, M. (1984). Methods Enzymol. 148, 403-415.
14. Elkeles, A., Breiman, A., and Zizi, M. (1997). J. Biol. Chem. 272, 6252-6260.
15. Fevre, F., Chich, J. F., Lauquin, G. J.-M., Henry, J. P., and Thieffry, M. (1990). FEBS Lett. 262, 201-204.
16. Guo, X. J. and Lauquin, G. J.-M. (1986). EBEC Rep. 4, 292.
17. Hill, K., Model, K., Ryan, M. T., Dietmeier, K., Martin, F., Wagner, R., and Pfanner, N. (1998). Nature (London) 395, 516-521.
18. Juin, P., Thieffry, M., Henry, J.-P., and Valletta, F. M. (1997). J. Biol. Chem. 272, 6044-6050.
19. Kamo, N., Maratsugu, M., Hongoh, R., and Kobatake, Y. J. (1979). J. Membr. Biol. 49, 105-121.
20. Kmita, H., Stobienia, O., and Michejda, J. (1999). Acta Biochim. Polon. 46, 991-1000.
21. Kmita, H. and Budzińska, M. (2000). Biochim. Biophys. Acta 1509, 86-94.
22. Kuenkele, K.-P., Heins, S., Dembowski, M., Nargang, F. E., Benz, R., Thieffry, M., Walz, J., Lill, R., Nussberger, S., and Neupert, W. (1998a). Cell 93, 1009-1019.
23. Kuenkele, K.-P., Juin, P., Pompa, C., Nargang, F. E., Henry, J.-P., Neupert, W., Lill, R., and Thieffry, M. (1998b). J. Biol. Chem. 273, 31032-31039.
24. Lämmli, U. K. (1970). Nature (London) 227, 680-685.
25. Lee, A. C., Zizi, M., and Colombini, M. (1994). J. Biol. Chem. 269, 30974-30980.
26. Lee, A. C., Xu, X., Blachly-Dyson, E., Forte, M., and Colombini, M. (1998). J. Membr. Biol. 161, 173-181.
27. Lill, R. and Neupert, W. (1996). Trends Cell Biol. 6, 56-61.
28. Mayer, A., Neupert, W., and Lill, R. (1995). Cell 80, 127-137.
29. Michejda, J., Guo, X. J., and Lauquin, G. J.-M. (1990). Biochem. Biophys. Res. Commun. 171, 354-361.
30. Michejda, J., Kmita, H., Stobienia, O., Budzińska, M., and Lauquin, G. J.-M. (1994). In Molecular Biology of Mitochondrial Transport System: Restriction of Metabolite Permeation through the Outer Mitochondrial Membrane of Porin-Deficient Yeast Mutant (Forte, M. and Colombini, M., eds.), Springer-Verlag, Heidelberg, pp. 341-356.
31. Rapaport, D., Neupert, W., and Lill, R. (1997). J. Biol. Chem. 272, 18725-18731.
32. Rapaport, D., Mayer, A., Neupert, W., and Lill, R. (1998). J. Biol. Chem. 273, 8806-8813.
33. Sampson, M. J., Lovell, R. S., and Craigen, W. J. (1997). J. Biol. Chem. 272, 18966-18973.
34. Schein, S. J., Colombini, M., and Finkelstein, A. V. (1976). J. Membr. Biol. 30, 99-120.
35. Sirrenberg, Ch., Endres, M., Becker, K., Bauer, M. F., Walther, E., Neupert, W., and Brunner, M. (1997). J. Biol. Chem. 272, 29963-29966.
36. Tarassov, I., Entelis, N., and Martin, R. P. (1995). J. Mol. Biol. 245, 315-323.
37. Thieffry, M., Chich, J. F., Goldschmidt, D., and Henry, J. P. (1988). EMBO J. 7, 1449-1454.
38. Thieffry, M., Fevre, F., Pelleschi, M., and Henry, J.-P. (1994). In Molecular Biology of Mitochondrial Transport Systems: The Mitochondrial Outer Membrane Contains at Least Two Distinct Channels (Forte, M. and Colombini, M., eds.), Springer-Verlag, Berlin.
39. Valletta, F. M., Juin, P., Peleschi, M., and Henry, J.-P. (1994). J. Biol. Chem. 269, 13367-13374.
40. Voos, W., Gambill, B. D., Laloraya, S., Ang, D., Graig, E. A., and Pfenner, N. (1994). Mol. Cell. Biol. 14, 6627-6634.
41. Wienhues, U., Koll, H., Becker, K., Guiard, B., and Haitl, F.-U. (1992). In Protein Targeting. Practical Approach: Protein Targeting to Mitochondria (Magge, A. and Wileman, T., eds.), Oxford University Press, London pp. 136-159.
42. Xu, X., Decker, W., Sampson, M. J., Craigen, W. J., and Colombini, M. (1999). J. Membr. Biol. 170, 89-102.
43. Zizi, M., Forte, M., Blachly-Dyson, E., and Colombini, M. (1994). J. Biol. Chem. 269, 1614-1616.