Skip to main content
SpringerLink
Log in

The Oligomycin Axis of Mitochondrial ATP Synthase: OSCP and the Proton Channel

  • Published:
Journal of Bioenergetics and Biomembranes Aims and scope Submit manuscript

Abstract

Oligomycin has long been known as an inhibitor of mitochondrial ATP synthase, putatively binding the Fo subunits 9 and 6 that contribute to proton channel function of the complex. As its name implies, OSCP is the oligomycin sensitivity-conferring protein necessary for the intact enzyme complex to display sensitivity to oligomycin. Recent advances concerning the structure and mechanism of mitochondrial ATP synthase have led to OSCP now being considered a component of the peripheral stator stalk rather than a central stalk component. How OSCP confers oligomycin sensitivity on the enzyme is unknown, but probably reflects important protein–protein interactions made within the assembled complex and transmitted down the stator stalk, thereby influencing proton channel function. We review here our studies directed toward establishing the stoichiometry, assembly, and function of OSCP in the context of knowledge of the organization of the stator stalk and the proton channel.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

REFERENCES

  • Abrahams, J. P., Leslie, A. G. W., Lutter, R., and Walker, J. E. (1994). Nature (London) 370, 621-628.

    Google Scholar 

  • Bateson, M., Devenish, R. J., Nagley, P., and Prescott, M. (1996). Anal. Biochem. 238, 14-18.

    Google Scholar 

  • Bateson, M., Devenish, R. J., Nagley, P., and Prescott, M. (1999). J. Biol. Chem. 274, 7462-7466.

    Google Scholar 

  • Bottcher, B., Schwartz, L., and Graber, P. (1998). J. Mol. Biol. 281, 757-762.

    Google Scholar 

  • Boyer, P. D. (1993). Biochim. Biophys. Acta 140, 215-250.

    Google Scholar 

  • Boyer, P. D. (1997). Annu. Rev. Biochem. 66, 717-749.

    Google Scholar 

  • Boyer, P. D. (1999). Nature (London) 402, 247-248.

    Google Scholar 

  • Boyle, G. M., Roucou, X., Nagley, P., Devenish, R. J., and Prescott, M. (2000). J. Bioenerg. Biomembr. 32, 469-481.

    Google Scholar 

  • Breen, G. A. M., Miller, D. L., Holmans, P. L., and Welch, G. (1986). J. Biol. Chem. 261, 11680-11685.

    Google Scholar 

  • Capaldi, R. A., Schulenberg, B., Murray, J., and Aggeler, R. (2000). J. Exp. Biol. 203, 29-33.

    Google Scholar 

  • Collinson, I. R., van Raaij, M. J., Runswick, M. J., Buchanan, S. K., Fearnley, I. M., Skehel, J. M., Orriss, G. L., Miroux, B., and Walker, J. E. (1994). J. Mol. Biol. 242, 408-421.

    Google Scholar 

  • Collinson, I. R., Skehel, J. M., Fearnley, I. M., Runswick, M. J., and Walker, J. E. (1996). Biochemistry 35, 12640-12646.

    Google Scholar 

  • Cox, G. B., Jans, D. A., Fimmel, A. L., Gibson, F., and Hatch, L. (1984). Biochim. Biophys. Acta 768, 201-208.

    Google Scholar 

  • Cox, G. B., Devenish, R. J., Gibson, F., Howitt, S. M., and Nagley, P. (1992). In Molecular Mechanisms in Bioenergetics (Ernster, L., ed.), Elsevier, Amsterdam, pp. 283-315.

    Google Scholar 

  • Deckers-Hebestreit, G., Greie, J.-C., Stalz, W.-D., and Altendorf, K. (2000). Biochim. Biophys. Acta 1458, 364-373.

    Google Scholar 

  • Devenish, R. J., Prescott, M., Roucou, X., and Nagley, P. (2000). Biochim. Biophys. Acta 1458, 428-442.

    Google Scholar 

  • Dimroth, P. (2000). Biochim. Biophys. Acta 1458, 374-386.

    Google Scholar 

  • Dupuis, A., Satre, M., and Vignais, P. V. (1983). FEBS Lett. 156, 99-102.

    Google Scholar 

  • Engelbrecht, S., and Junge, W. (1997). FEBS Lett. 414, 485-491.

    Google Scholar 

  • Fillingame, R. H. (1997). J. Exp. Biol. 200, 217-224.

    Google Scholar 

  • Fillingame, R. H. (1999). Science 286, 1687-1688.

    Google Scholar 

  • Fillingame, R. H., Jiang, W., Dmitriev, O. Y., Jones, P. C. (2000). Biochim. Biophys. Acta 1458, 387-403.

    Google Scholar 

  • Galanis, M., Mattoon, J. R., and Nagley, P. (1989). FEBS Lett. 249, 333-336.

    Google Scholar 

  • Girvan, M. E., Rastogi, V. K., Abildgaard, F., Markley, J. L. and Fillingame, R. H. (1998). Biochemistry 37, 8817-8824.

    Google Scholar 

  • Golden, T. R., and Pedersen, P. L. (1998). Biochemistry 37, 13871-13881.

    Google Scholar 

  • Groth, G. (2000). Biochim. Biophys. Acta 1458, 417-427.

    Google Scholar 

  • Hadikusumo, R. G., Hertzog, P. J., and Marzuki, S. (1984). Biochim. Biophys. Acta 765, 258-267.

    Google Scholar 

  • Hazard, A. L., and Senior, A. E. (1994). J. Biol. Chem. 269, 427-432.

    Google Scholar 

  • Hekman, C., Tomich, J. M., and Hatefi, Y. (1991). J. Biol. Chem. 266, 13564-13571.

    Google Scholar 

  • John, U. P., and Nagley, P. (1986). FEBS Lett. 207, 79-83.

    Google Scholar 

  • Joshi, S., Cao, G-J., Nath, C., and Shah, J. (1996). Biochemistry 35, 12094-12103.

    Google Scholar 

  • Joshi, S., Cao, G-J., Nath, C., and Shah, J. (1997). Biochemistry 36, 10936-10943.

    Google Scholar 

  • Karrasch, S., and Walker, J. E., (1999). J. Mol. Biol. 290, 379-384.

    Google Scholar 

  • Kato-Yamada, Y., Noji, H., Yasuda, R., Kinosita Jr., K., and Yoshida, M. (1998). J. Biol. Chem. 273, 19375-19377.

    Google Scholar 

  • Law, R. H. P., Manon, S., Devenish, R. J., and Nagley, P. (1995). Methods Enzymol. 260, 133-163.

    Google Scholar 

  • Macino, G., and Tzagoloff, A. (1980). Cell 20, 507-517.

    Google Scholar 

  • Mao, Y., and Mueller, D. M. (1997). Arch. Biochem. Biophys. 337, 8-16.

    Google Scholar 

  • McLachlin, D. T., Coveny, A. M., Clark, S. M., and Dunn, S. D. (2000). J. Biol. Chem. 275, 17571-17577.

    Google Scholar 

  • Mukopadhyay, A., Zhou, X-Q., Uh, M., and Mueller, D. M. (1992). J. Biol. Chem. 267, 25690-25696.

    Google Scholar 

  • Nagley, P. (1988). Trends Genet. 4, 46-52.

    Google Scholar 

  • Nagley, P., Hall, R. M., and Ooi, B. G. (1986). FEBS Lett. 195, 159-163.

    Google Scholar 

  • Nagley, P., and Linnane, A. W. (1987). In Bioenergetics: Structure and Function of Energy Transducing Systems (Ozawa, T., and Papa, S., eds), Japan Scientific Societies Press, Tokyo and Springer-Verlag, Berlin, pp. 191-204.

    Google Scholar 

  • Noji, H., Yasuda, R., Yoshida, M., and Kinosita Jr., K. (1997). Nature (London) 386, 299-302.

    Google Scholar 

  • Ogilvie, I., Aggeler, R., and Capaldi, R. A. (1997). J. Biol. Chem. 272, 16652-16656.

    Google Scholar 

  • Ooi, B. G., Novitski, C. E., and Nagley, P. (1985). Eur. J. Biochem. 152, 709-714.

    Google Scholar 

  • Ovchinnikov, Y. A., Modyanov, N. N., Grinkevich, V. A., Aldanova, N. A., Trubetskaya, O. E., Hundal, T., and Ernster, L. (1984a). FEBS Lett. 166, 19-22.

    Google Scholar 

  • Ovchinnikov, Y. A., Modyanov, N. N., Grinkevich, V. A., Kostetsky, P. V., Trubetskaya, O. E., Hundal, T., and Ernster, L. (1984b). FEBS Lett. 175, 109-112.

    Google Scholar 

  • Penin, F., Archinard, P., Moradi-Ameli, M., and Godinot, C. (1985). Biochim. Biophys. Acta 810, 346-353.

    Google Scholar 

  • Perlin, D. S., Latchney, L. R., and Senior, A. E. (1985). Biochim. Biophys. Acta 807, 238-244.

    Google Scholar 

  • Prescott, M., Bush, N., Nagley, P., and Devenish, R. J. (1994). Biochem. Mol. Biol. Int. 34, 789-799.

    Google Scholar 

  • Prescott, M., Higuti, T., Nagley, P., and Devenish, R. J. (1995). Biochem. Biophys. Res. Commun. 207, 943-949.

    Google Scholar 

  • Prescott, M., Devenish, R. J., and Nagley, P. (1996). In Protein targeting to mitochondria (Hartl, F.-U., ed.), JAI Press, Greenwich, Connecticut, pp. 299-339.

    Google Scholar 

  • Pringle, M. J., Kenneally, M. K., and Joshi, S. (1990). J. Biol. Chem. 265, 7632-7637.

    Google Scholar 

  • Rodgers, A. J. W., and Capaldi, R. A. (1998). J. Biol. Chem. 273, 29406-29410.

    Google Scholar 

  • Roucou, X., Artika, I. M., Devenish, R. J., and Nagley, P. (1999). Eur. J. Biochem. 261, 444-451.

    Google Scholar 

  • Sambongi, Y., Iko, Y., Tanabe, M., Omote, H., Iwamoto-Kihara, A., Ueda, I., Yanagida, T., Wada, Y., and Futai, M. (1999). Science 286, 1722-1724.

    Google Scholar 

  • Sebald, W., Wachter, E., and Tzagoloff, A. (1979). Eur. J. Biochem. 100, 599-607.

    Google Scholar 

  • Slater, E. C. (1967). Methods Enzymol. X, 48-57.

    Google Scholar 

  • Slott, E. F., Shade, R. O., and Lansman, R. A. (1983). Mol. Cell. Biol. 3, 1694-1702.

    Google Scholar 

  • Soubannier, V., Rusconi, F., Vaillier, J., Arselin, G., Chaignepain, S., Graves, P. V., Schmitter, J. M., Zhang, J. L., Mueller, D., and Velours, J. (1999). Biochemistry 38, 15017-15024.

    Google Scholar 

  • Spannagel, C., Vaillier, J., Chaignepain, S., and Velours, J. (1998). Biochemistry 37, 615-621.

    Google Scholar 

  • Stephens, A. N., Roucou, X., Artika, I. M., Devenish, R. J., and Nagley, P. (2000). Eur. J. Biochem. 267, 6443-6451.

    Google Scholar 

  • Stock, D., Leslie, A. G. W., and Walker, J. E. (1999). Science 286, 1700-1705.

    Google Scholar 

  • Straffon, A. F. L., Prescott, M., Nagley, N., and Devenish, R. J. (1998). Biochim. Biophys. Acta 1371, 157-162.

    Google Scholar 

  • Svergun, D. I., Aldag, I., Sieck, T., Altendorf, K., Koch, M. H. J., Kane, D. J., Kozin, M. B., and Gruber, G. (1998). Biophys. J. 75, 2212-2219.

    Google Scholar 

  • Tzagoloff, A. (1970). J. Biol. Chem. 245, 1545-1551.

    Google Scholar 

  • Velours, J., Spannagel, C., Chaignepain, S., Vaillier, J., Arselin, G., Graves, P. V., Velours, G., and Camougrand, N. (1998). Biochimie 80, 793-801.

    Google Scholar 

  • Velours, J., Paumard, P., Soubannier, V., Spannagel, C., Vaillier, J., Arselin, G., and Graves, P.-V. (2000). Biochim. Biophys. Acta 1458, 443-456.

    Google Scholar 

  • Vik, S. B., Long, J. C., Wada, T., and Zhang, D. (2000). Biochim. Biophys. Acta 1458, 457-466.

    Google Scholar 

  • Weber, J., and Senior, A. E. (1997). Biochim. Biophys. Acta 1319, 19-58.

    Google Scholar 

  • Willson T. W., and Nagley, P. (1987). Eur. J. Biochem. 167, 291-297.

    Google Scholar 

  • Wilkens, S., and Capaldi, R. A. (1998). Nature (London) 393, 29.

    Google Scholar 

  • Wilkens, S., Zhou, J., Nakayama, R., Dunn, S. D., and Capaldi, R. A. (2000). J. Mol. Biol. 295, 387-391.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, Monash University, P.O. Box 13D, Victoria, 3800, Australia

    Rodney J. Devenish & Mark Prescott

  2. Queensland Institute of Medical Research, Herston, Queensland, 4006, Australia

    Glen M. Boyle

  3. Department of Biochemistry and Molecular Biology, Monash University, P.O. Box 13D, Victoria, 3800, Australia

    Phillip Nagley

Authors
  1. Rodney J. Devenish
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Mark Prescott
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Glen M. Boyle
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Phillip Nagley
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Devenish, R.J., Prescott, M., Boyle, G.M. et al. The Oligomycin Axis of Mitochondrial ATP Synthase: OSCP and the Proton Channel. J Bioenerg Biomembr 32, 507–515 (2000). https://doi.org/10.1023/A:1005621125812

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1005621125812

Search

Navigation