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Aerolysin, a hemolysin fromAeromonas hydrophila, forms voltage-gated channels in planar lipid bilayers

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Summary

The cytolytic toxin aerolysin was found to form ion channels which displayed slight anion selectivity in planar lipid bilayers. In voltage-clamp experiments the ion current flowing through the channels was homogeneous indicating a defined conformation and a uniform size. The channels remained open between −70 to +70 mV, but outside this range they underwent voltage-dependent inactivation which was observed as open-closed fluctuations at the single-channel level. Zinc ions not only prevented the formation of channels by inhibiting oligomerization of monomeric aerolysin but they also induced a closure of preformed channels in a voltage-dependent fashion. The results of a Hill plot indicated that 2–3 zinc ions bound to a site within the channel lumen. Proaerolysin, and a mutant of aerolysin in which histidine 132 was replaced by an asparagine, were both unable to oligomerize and neither could form channels. This is evidence that oligomerization is a necessary step in channel formation.

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Authors and Affiliations

  1. European Molecular Biology Laboratory, 6900, Heidelberg, Germany

    H. U. Wilmsen & F. Pattus

  2. Department of Biochemistry and Microbiology, University of Victoria, V8W 2Y2, Victoria, British Columbia, Canada

    J. T. Buckley

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  1. H. U. Wilmsen
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  2. F. Pattus
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  3. J. T. Buckley
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Wilmsen, H.U., Pattus, F. & Buckley, J.T. Aerolysin, a hemolysin fromAeromonas hydrophila, forms voltage-gated channels in planar lipid bilayers. J. Membrain Biol. 115, 71–81 (1990). https://doi.org/10.1007/BF01869107

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  • DOI: https://doi.org/10.1007/BF01869107

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