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

DC FieldValueLanguage
dc.contributor.authorDunkel, S.
dc.contributor.authorPulagam, L. P.
dc.contributor.authorSteinhoff, H. -J.
dc.contributor.authorKlare, J. P.
dc.date.accessioned2021-12-23T16:03:31Z-
dc.date.available2021-12-23T16:03:31Z-
dc.date.issued2015
dc.identifier.issn14639076
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/6045-
dc.description.abstractWe 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.
dc.description.sponsorshipDFG priority programGerman Research Foundation (DFG) [SPP1601]; We acknowledge the DFG priority program SPP1601 for financial support.
dc.language.isoen
dc.publisherROYAL SOC CHEMISTRY
dc.relation.ispartofPHYSICAL CHEMISTRY CHEMICAL PHYSICS
dc.subjectChemistry
dc.subjectChemistry, Physical
dc.subjectELECTRON
dc.subjectHELICES
dc.subjectIA CHANNEL
dc.subjectMUTANTS
dc.subjectPhysics
dc.subjectPhysics, Atomic, Molecular & Chemical
dc.subjectPROTEINS
dc.subjectREDUCTION
dc.subjectRESONANCE
dc.subjectSTATE
dc.subjectTOPOLOGY
dc.subjectTRANSLOCATION
dc.titleIn vivo EPR on spin labeled colicin A reveals an oligomeric assembly of the pore-forming domain in E. coli membranes
dc.typejournal article
dc.identifier.doi10.1039/c4cp05638h
dc.identifier.isiISI:000349616400008
dc.description.volume17
dc.description.issue7
dc.description.startpage4875
dc.description.endpage4878
dc.contributor.orcid0000-0002-5888-0157
dc.contributor.orcid0000-0002-5761-5968
dc.contributor.researcheridH-3791-2014
dc.contributor.researcheridC-1428-2009
dc.identifier.eissn14639084
dc.publisher.placeTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND
dcterms.isPartOf.abbreviationPhys. Chem. Chem. Phys.
dcterms.oaStatusGreen Submitted, hybrid
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