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Colicin Occlusion of OmpF and TolC Channels: Outer Membrane Translocons for Colicin Import
Journal article   Open access   Peer reviewed

Colicin Occlusion of OmpF and TolC Channels: Outer Membrane Translocons for Colicin Import

Stanislav D. Zakharov, Veronika Y. Eroukova, Tatyana I. Rokitskaya, Mariya V. Zhalnina, Onkar Sharma, Patrick J. Loll, Helen I. Zgurskaya, Yuri N. Antonenko and William A. Cramer
Biophysical journal, v 87(6), pp 3901-3911
01 Oct 2004
DOI: https://doi.org/10.1529/biophysj.104.046151
PMID: 15465872
Featured in Collection :   UN Sustainable Development Goals @ Drexel
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https://doi.org/10.1529/biophysj.104.046151View
Published, Version of Record (VoR)Open Access (Publisher-Specific),  Open

Abstract

Membranes
The interaction of colicins with target cells is a paradigm for protein import. To enter cells, bactericidal colicins parasitize Escherichia coli outer membrane receptors whose physiological purpose is the import of essential metabolites. Colicins E1 and E3 initially bind to the BtuB receptor, whose β -barrel pore is occluded by an N-terminal globular “plug”. The x-ray structure of a complex of BtuB with the coiled-coil BtuB-binding domain of colicin E3 did not reveal displacement of the BtuB plug that would allow passage of the colicin (Kurisu, G., S. D. Zakharov, M. V. Zhalnina, S. Bano, V. Y. Eroukova, T. I. Rokitskaya, Y. N. Antonenko, M. C. Wiener, and W. A. Cramer. 2003. Nat. Struct. Biol. 10:948–954). This correlates with the inability of BtuB to form ion channels in planar bilayers, shown in this work, suggesting that an additional outer membrane protein(s) is required for colicin import across the outer membrane. The identity and interaction properties of this OMP were analyzed in planar bilayer experiments.OmpF and TolC channels in planar bilayers were occluded by colicins E3 and E1, respectively, from the trans- side of the membrane. Occlusion was dependent upon a cis- negative transmembrane potential. A positive potential reversibly opened OmpF and TolC channels. Colicin N, which uses only OmpF for entry, occludes OmpF in planar bilayers with the same orientation constraints as colicins E1 and E3. The OmpF recognition sites of colicins E3 and N, and the TolC recognition site of colicin E1, were found to reside in the N-terminal translocation domains. These data are considered in the context of a two-receptor translocon model for colicin entry into cells.

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Web of Science research areas
Biophysics
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