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

Autor(en): Dunkel, S.
Pulagam, L. P.
Steinhoff, H. -J.
Klare, J. P.
Stichwörter: Chemistry; Chemistry, Physical; ELECTRON; HELICES; IA CHANNEL; MUTANTS; Physics; Physics, Atomic, Molecular & Chemical; PROTEINS; REDUCTION; RESONANCE; STATE; TOPOLOGY; TRANSLOCATION
Erscheinungsdatum: 2015
Herausgeber: ROYAL SOC CHEMISTRY
Journal: PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volumen: 17
Ausgabe: 7
Startseite: 4875
Seitenende: 4878
Zusammenfassung: 
We report on the application of site-directed spin labeling (SDSL) and electron paramagnetic resonance (EPR) 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.
ISSN: 14639076
DOI: 10.1039/c4cp05638h

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