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Purification and characterization of the pore forming protein of yeast mitochondrial outer membrane

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Abstract

One of the major outer membrane proteins of yeast mitochondria was isolated and purified. It migrated as a single band with an apparent molecular weight of 30 kDa on a SDS-electrophoretogram. When reconstituted in lipid bilayer membranes the protein formed pores with a single channel conductance of 0.45 nS in 0.1 M KCl. The pores had the characteristics of general diffusion pores with an estimated diameter of 1.7 nm. The pore of mitochondrial outer membranes of yeast shared some similarities with the pores formed by mitochondrial and bacterial porins. The pores switched to substates at voltages higher than 20 mV. The possible role of this voltagedependence in the metabolism of mitochondria is discussed.

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Authors and Affiliations

  1. Lehrstuhl für Biotechnologie, Universität Würzburg, Röntgenring 11, D-8700, Würzburg, Germany

    O. Ludwig & R. Benz

  2. Dr. Karl Thomae, Abteilung-Biochemie, Postfach 1755, D-7950, Biberach, Germany

    J. Krause

  3. Department of Pathology, University of Chicago, 55841 South Maryland Avenue, 60637, Chicago, IL, USA

    R. Hay

Authors
  1. O. Ludwig
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  2. J. Krause
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  3. R. Hay
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  4. R. Benz
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Ludwig, O., Krause, J., Hay, R. et al. Purification and characterization of the pore forming protein of yeast mitochondrial outer membrane. Eur Biophys J 15, 269–276 (1988). https://doi.org/10.1007/BF00256477

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  • DOI: https://doi.org/10.1007/BF00256477

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