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Lipid Headgroup Charge and Acyl Chain Composition Modulate Closure of Bacterial β-Barrel Channels
dc.contributor.author | Perini, Deborah Aurora | |
dc.contributor.author | Alcaraz, Antonio | |
dc.contributor.author | Queralt-Martín, María | |
dc.date.accessioned | 2019-05-17T07:08:12Z | |
dc.date.available | 2019-05-17T07:08:12Z | |
dc.date.issued | 2019-02 | |
dc.identifier.citation | Perini, D.A.; Alcaraz, A.; Queralt-Martín, M. Lipid Headgroup Charge and Acyl Chain Composition Modulate Closure of Bacterial β-Barrel Channels. Int. J. Mol. Sci. 2019, 20, 674. | ca_CA |
dc.identifier.uri | http://hdl.handle.net/10234/182517 | |
dc.description.abstract | The outer membrane of Gram-negative bacteria contains β-barrel proteins that form high-conducting ion channels providing a path for hydrophilic molecules, including antibiotics. Traditionally, these proteins have been considered to exist only in an open state so that regulation of outer membrane permeability was accomplished via protein expression. However, electrophysiological recordings show that β-barrel channels respond to transmembrane voltages by characteristically switching from a high-conducting, open state, to a so-called ‘closed’ state, with reduced permeability and possibly exclusion of large metabolites. Here, we use the bacterial porin OmpF from E. coli as a model system to gain insight on the control of outer membrane permeability by bacterial porins through the modulation of their open state. Using planar bilayer electrophysiology, we perform an extensive study of the role of membrane lipids in the OmpF channel closure by voltage. We pay attention not only to the effects of charges in the hydrophilic lipid heads but also to the contribution of the hydrophobic tails in the lipid-protein interactions. Our results show that gating kinetics is governed by lipid characteristics so that each stage of a sequential closure is different from the previous one, probably because of intra- or intermonomeric rearrangements. | ca_CA |
dc.format.extent | 12 p. | ca_CA |
dc.format.mimetype | application/pdf | ca_CA |
dc.language.iso | eng | ca_CA |
dc.publisher | MDPI | ca_CA |
dc.rights | © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license . | ca_CA |
dc.rights | Atribución 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-sa/4.0/ | * |
dc.subject | bacterial porins | ca_CA |
dc.subject | voltage gating | ca_CA |
dc.subject | beta-barrel channel | ca_CA |
dc.subject | phospholipids | ca_CA |
dc.subject | lipid headgroup charge | ca_CA |
dc.subject | hydrophobic acyl chains | ca_CA |
dc.title | Lipid Headgroup Charge and Acyl Chain Composition Modulate Closure of Bacterial β-Barrel Channels | ca_CA |
dc.type | info:eu-repo/semantics/article | ca_CA |
dc.identifier.doi | https://doi.org/10.3390/ijms20030674 | |
dc.relation.projectID | Spanish Government (FIS2016-75257-P AEI/FEDER) ; Universitat Jaume I (P1.1B2015-28 and UJI-B2018-53) | ca_CA |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | ca_CA |
dc.relation.publisherVersion | https://www.mdpi.com/1422-0067/20/3/674 | ca_CA |
dc.contributor.funder | Intramural Research Program of the National Institutes of Health, Eunice Kennedy Shriver National Institute of Child Health and Human Development (Bethesda, MD) | ca_CA |
dc.type.version | info:eu-repo/semantics/publishedVersion | ca_CA |
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