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Detergent-labile, supramolecular assemblies of KcsA: relative abundance and interactions involved

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dc.contributor.authorGiudici Besseghini, Ana Marcela
dc.contributor.authorMolina Gallego, María Luisa
dc.contributor.authorAyala Torres, José Leonardo
dc.contributor.authorMontoya Díaz, Estefanía
dc.contributor.authorRenart Pérez, María Lourdes
dc.contributor.authorFernández Carvajal, Asia María
dc.contributor.authorEncinar Hidalgo, José Antonio
dc.contributor.authorFerrer Montiel, Antonio Vicente
dc.contributor.authorPoveda Larrosa, José Antonio
dc.contributor.authorGonzález Ros, José Manuel
dc.contributor.departmentBioquímica y Biología Molecular B e Inmunología
dc.date.accessioned2024-07-03T11:46:04Z
dc.date.available2024-07-03T11:46:04Z
dc.date.issued2012-09-27
dc.description© 2012 Elsevier B.V. All rights reserved. This document is the Published version of a Published Work that appeared in final form in Biochimica et Biophysica Acta (BBA) - Bioenergetics. To access the final edited and published work see https://doi.org/10.1016/j.bbamem.2012.09.020
dc.description.abstractIn this work, we illustrate the ability of the prokaryotic potassium channel KcsA to assemble into a variety of supramolecular clusters of defined sizes containing the tetrameric KcsA as the repeating unit. Such clusters, particularly the larger ones, are markedly detergent-labile and thus, disassemble readily upon exposure to the detergents commonly used in protein purification or conventional electrophoresis analysis. This is a reversible process, as cluster re-assembly occurs upon detergent removal and without the need of added membrane lipids. Interestingly, the dimeric ensemble between two tetrameric KcsA molecules are quite resistant to detergent disassembly to individual KcsA tetramers and along with the latter, are likely the basic building blocks through which the larger clusters are organized. As to the proteins domains involved in clustering, we have observed disassembly of KcsA clusters by SDS-like alkyl sulfates. As these amphiphiles bind to inter-subunit, “non-annular” sites on the protein, these observations suggest that such sites also mediate channel–channel interactions leading to cluster assembly.es
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dc.format.extent8es
dc.identifier.citationBiochimica et Biophysica Acta 1828 (2013) 193–200
dc.identifier.doihttps://doi.org/10.1016/j.bbamem.2012.09.020
dc.identifier.issnPrint: 0005-2728
dc.identifier.issnElectronic: 1879-2650
dc.identifier.urihttp://hdl.handle.net/10201/142850
dc.languageenges
dc.publisherElsevieres
dc.relationPartly supported by grants from the Spanish MICINN BFU2008-0062/BMC, BFU2009-08346, BFU2011-25920 and Consolider-Ingenio 2010 CSD2-2008-00005, and from the Generalitat Valenciana Prometeo 2010/046.es
dc.relation.publisherversionhttps://www.sciencedirect.com/science/article/pii/S0005273612003410?via%3Dihub
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectIon channels supramolecular assemblyes
dc.subjectProtein clusterses
dc.subjectDetergent stabilityes
dc.subjectCrosslinkinges
dc.subjectBlue native PAGEes
dc.subjectMembrane proteins “non-annular” siteses
dc.titleDetergent-labile, supramolecular assemblies of KcsA: relative abundance and interactions involvedes
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
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