Lipid Headgroup Charge and Acyl Chain Composition Modulate Closure of Bacterial β-Barrel Channels
Impacto
Scholar |
Otros documentos de la autoría: perini, deborah aurora; Alcaraz, Antonio; Queralt-Martín, María
Metadatos
Mostrar el registro completo del ítemcomunitat-uji-handle:10234/9
comunitat-uji-handle2:10234/2507
comunitat-uji-handle3:10234/6973
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INVESTIGACIONMetadatos
Título
Lipid Headgroup Charge and Acyl Chain Composition Modulate Closure of Bacterial β-Barrel ChannelsFecha de publicación
2019-02Editor
MDPICita bibliográfica
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.Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
https://www.mdpi.com/1422-0067/20/3/674Versión
info:eu-repo/semantics/publishedVersionPalabras clave / Materias
Resumen
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 ... [+]
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. [-]
Proyecto de investigación
Spanish Government (FIS2016-75257-P AEI/FEDER) ; Universitat Jaume I (P1.1B2015-28 and UJI-B2018-53)Derechos de acceso
info:eu-repo/semantics/openAccess
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