Confined Mobility of TonB and FepA in Escherichia coli Membranes

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dc.contributor.authorYoriko Lill
dc.contributor.authorLorne D. Jordan
dc.contributor.authorChuck R. Smallwood
dc.contributor.authorSalete M. Newton
dc.contributor.authorMarkus A. Lill
dc.contributor.authorPhillip E. Klebba
dc.contributor.authorKen Ritchie
dc.date.accessioned2017-03-05T23:40:57Z
dc.date.available2017-03-05T23:40:57Z
dc.date.issued2016-12-09
dc.descriptionen_US
dc.descriptionen_US
dc.description.abstractThe important process of nutrient uptake in Escherichia coli, in many cases, involves transit of the nutrient through a class of beta-barrel proteins in the outer membrane known as TonB-dependent transporters (TBDTs) and requires interaction with the inner membrane protein TonB. Here we have imaged the mobility of the ferric enterobactin transporter FepA and TonB by tracking them in the membranes of live E. coli with single-molecule resolution at time-scales ranging from milliseconds to seconds. We employed simple simulations to model/analyze the lateral diffusion in the membranes of E.coli, to take into account both the highly curved geometry of the cell and artifactual effects expected due to finite exposure time imaging. We find that both molecules perform confined lateral diffusion in their respective membranes in the absence of ligand with FepA confined to a region 0.180−0.007+0.006 μm in radius in the outer membrane and TonB confined to a region 0.266−0.009+0.007 μm in radius in the inner membrane. The diffusion coefficient of these molecules on millisecond time-scales was estimated to be 21−5+9 μm2/s and 5.4−0.8+1.5 μm2/s for FepA and TonB, respectively, implying that each molecule is free to diffuse within its domain. Disruption of the inner membrane potential, deletion of ExbB/D from the inner membrane, presence of ligand or antibody to FepA and disruption of the MreB cytoskeleton was all found to further restrict the mobility of both molecules. Results are analyzed in terms of changes in confinement size and interactions between the two proteins.en_US
dc.description.peerreviewYesen_US
dc.description.peerreviewnoteshttp://www.plosone.org/static/editorial#peeren_US
dc.identifier.citationLill Y, Jordan LD, Smallwood CR, Newton SM, Lill MA, Klebba PE, et al. (2016) Confined Mobility of TonB and FepA in Escherichia coli Membranes. PLoS ONE 11(12): e0160862. doi:10.1371/journal.pone.0160862en_US
dc.identifier.doi10.1371/journal.pone.0160862en_US
dc.identifier.urihttp://hdl.handle.net/11244/49294
dc.language.isoen_USen_US
dc.publisherPLos One
dc.relation.ispartofseriesPLoS ONE 11(12): e0160862
dc.relation.urihttp://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0160862
dc.rightsAttribution 3.0 United States
dc.rights.requestablefalseen_US
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/
dc.subjectMass diffusivity,Fluorescence imaging,Outer membrane proteins,Monte Carlo method,Radii,Cell disruption,Membrane potential,Simulation and modelingen_US
dc.titleConfined Mobility of TonB and FepA in Escherichia coli Membranesen_US
dc.typeResearch Articleen_US

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