Voltage-dependent gating properties of the channel formed by E. coli hemolysin in planar lipid membranes
- 1 August 1989
- journal article
- research article
- Published by Portland Press Ltd. in Bioscience Reports
- Vol. 9 (4) , 465-473
- https://doi.org/10.1007/bf01117049
Abstract
Escherichia coli hemolysin forms cation selective, ion-permeable channels of large conductance in planar phospholipid bilayer membranes. The pore formation mechanism is voltage dependent resembling that of some colicins and of diphtheria toxin: pores open when negative voltages are applied and close with positive potentials. The pH dependence of this gating process suggests that it is mediated by a negative fixed charge present in the lumen of the pore. A simple physical model of how the channel opens and closes in response to the applied voltage is given.Keywords
This publication has 13 references indexed in Scilit:
- The hemolysin of escherichia coliEuropean Journal of Epidemiology, 1988
- Escherichia coli hemolysin permeabilizes small unilamellar vesicles loaded with calcein by a single‐hit mechanismFEBS Letters, 1988
- Escherichia coli haemolysin forms voltage-dependent ion channels in lipid membranesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1987
- Escherichia coli hemolysin may damage target cell membranes by generating transmembrane poresInfection and Immunity, 1986
- Purification of α-hemolysin from an overproducing E. coli strainMolecular Genetics and Genomics, 1985
- Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: relevance to translocation of proteins across membranes.Proceedings of the National Academy of Sciences, 1985
- A novel mechanism for voltage control of channel conductanceJournal of Theoretical Biology, 1984
- Studies on the mechanism of action of channel-forming colicins using artificial membranesThe Journal of Membrane Biology, 1984
- Escherichia coli alpha-hemolysin: characteristics and probable role in pathogenicity.Microbiological Reviews, 1984
- Colicin K acts by forming voltage-dependent channels in phospholipid bilayer membranesNature, 1978