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Issue 7, 2015
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In vivo EPR on spin labeled colicin A reveals an oligomeric assembly of the pore-forming domain in E. coli membranes

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Abstract

We report on the application of site-directed spin labeling (SDSL) and electron paramagnetic resonance (EPR) spectroscopy to study possible oligomerization of the bacterial toxin colicin A (ColA) upon membrane insertion in vitro and in vivo. We applied SDSL-EPR protocols and optimized experimental conditions to perform continuous wave EPR experiments and double electron–electron resonance distance measurements on intact Escherichia coli cells interacting with nitroxide spin-labeled ColA. Our data suggest that ColA forms dimers upon membrane insertion, thus explaining previously reported pore diameters of about 1 nm, which are unlikely to be formed by a single colicin A monomer.

Graphical abstract: In vivo EPR on spin labeled colicin A reveals an oligomeric assembly of the pore-forming domain in E. coli membranes

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Publication details

The article was received on 04 Dec 2014, accepted on 16 Jan 2015 and first published on 16 Jan 2015


Article type: Communication
DOI: 10.1039/C4CP05638H
Citation: Phys. Chem. Chem. Phys., 2015,17, 4875-4878
  • Open access: Creative Commons BY-NC license
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    In vivo EPR on spin labeled colicin A reveals an oligomeric assembly of the pore-forming domain in E. coli membranes

    S. Dunkel, L. P. Pulagam, H.-J. Steinhoff and J. P. Klare, Phys. Chem. Chem. Phys., 2015, 17, 4875
    DOI: 10.1039/C4CP05638H

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