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dc.creatorBernal Guzmán, Patriciaes
dc.creatorFurniss, R. Christopher D.es
dc.creatorFecht, Selinaes
dc.creatorLeung, Rhoda C. Y.es
dc.creatorSpiga, Liviaes
dc.creatorMavridou, Despoina A. I.es
dc.creatorFilloux, Alaines
dc.date.accessioned2021-02-15T13:32:11Z
dc.date.available2021-02-15T13:32:11Z
dc.date.issued2021
dc.identifier.citationBernal Guzmán, P., Furniss, R.C.D., Fecht, S., Leung, R.C.Y., Spiga, L., Mavridou, D.A.I. y Filloux, A. (2021). A novel stabilization mechanism for the type VI secretion system sheath. Proceedings of the National Academy of Sciences, 118 (7), 2008500118.
dc.identifier.issn0027-8424 (impreso)es
dc.identifier.issn1091-6490 (electrónico)es
dc.identifier.urihttps://hdl.handle.net/11441/104967
dc.description.abstractThe type VI secretion system (T6SS) is a phage-derived contractile nanomachine primarily involved in interbacterial competition. Its pivotal component, TssA, is indispensable for the assembly of the T6SS sheath structure, the contraction of which propels a payload of effector proteins into neighboring cells. Despite their key function, TssA proteins exhibit unexpected diversity and exist in two major forms, a short form (TssAS) and a long form (TssAL). While TssAL proteins interact with a partner, called TagA, to anchor the distal end of the extended sheath, the mechanism for the stabilization of TssAS-containing T6SSs remains unknown. Here we discover a class of structural components that interact with short TssA proteins and contribute to T6SS assembly by stabilizing the polymerizing sheath from the baseplate. We demonstrate that the presence of these components is important for full sheath extension and optimal firing. Moreover, we show that the pairing of each form of TssA with a different class of sheath stabilization proteins results in T6SS apparatuses that either reside in the cell for some time or fire immediately after sheath extension. We propose that this diversity in firing dynamics could contribute to the specialization of the T6SS to suit bacterial lifestyles in diverse environmental niches.es
dc.formatapplication/pdfes
dc.format.extent9 p.es
dc.language.isoenges
dc.publisherNational Academy of Scienceses
dc.relation.ispartofProceedings of the National Academy of Sciences, 118 (7), 2008500118.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectType VI secretion systemes
dc.subjectTssAes
dc.subjectTagBes
dc.subjectSheath stabilizationes
dc.subjectPseudomonases
dc.titleA novel stabilization mechanism for the type VI secretion system sheathes
dc.typeinfo:eu-repo/semantics/articlees
dc.type.versioninfo:eu-repo/semantics/publishedVersiones
dc.rights.accessrightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Microbiologíaes
dc.relation.publisherversionhttps://doi.org/10.1073/pnas.2008500118es
dc.identifier.doi10.1073/pnas.2008500118 |es
dc.journaltitleProceedings of the National Academy of Scienceses
dc.publication.volumen118es
dc.publication.issue7es
dc.publication.initialPage2008500118es
dc.publication.endPagees

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