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dc.rights.licenseopenen_US
dc.contributor.authorCHERRAK, Yassine
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorRAPISARDA, Chiara
dc.contributor.authorPELLARIN, Riccardo
dc.contributor.authorBOUVIER, Guillaume
dc.contributor.authorBARDIAUX, Benjamin
dc.contributor.authorALLAIN, Fabrice
dc.contributor.authorMALOSSE, Christian
dc.contributor.authorREY, Martial
dc.contributor.authorCHAMOT-ROOKE, Julia
dc.contributor.authorCASCALES, Eric
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorFRONZES, Rémi
dc.contributor.authorDURAND, Eric
dc.date.accessioned2024-09-30T09:39:32Z
dc.date.available2024-09-30T09:39:32Z
dc.date.issued2018-12-01
dc.identifier.issn2058-5276en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/202019
dc.description.abstractEnTo support their growth in a competitive environment and cause pathogenesis, bacteria have evolved a broad repertoire of macromolecular machineries to deliver specific effectors and toxins. Among these multiprotein complexes, the type VI secretion system (T6SS) is a contractile nanomachine that targets both prokaryotic and eukaryotic cells. The T6SS comprises two functional subcomplexes: a bacteriophage-related tail structure anchored to the cell envelope by a membrane complex. As in other contractile injection systems, the tail is composed of an inner tube wrapped by a sheath and built on the baseplate. In the T6SS, the baseplate is not only the tail assembly platform, but also docks the tail to the membrane complex and hence serves as an evolutionary adaptor. Here we define the biogenesis pathway and report the cryo-electron microscopy (cryo-EM) structure of the wedge protein complex of the T6SS from enteroaggregative Escherichia coli (EAEC). Using an integrative approach, we unveil the molecular architecture of the whole T6SS baseplate and its interaction with the tail sheath, offering detailed insights into its biogenesis and function. We discuss architectural and mechanistic similarities but also reveal key differences with the T4 phage and Mu phage baseplates.
dc.language.isoENen_US
dc.subject.enBacteriophages
dc.subject.enCell Membrane
dc.subject.enCryoelectron Microscopy
dc.subject.enEscherichia coli
dc.subject.enEscherichia coli Proteins
dc.subject.enModels
dc.subject.enMolecular
dc.subject.enMultiprotein Complexes
dc.subject.enProtein Conformation
dc.subject.enProtein Conformation
dc.subject.enalpha-Helical
dc.subject.enProtein Interaction Domains and Motifs
dc.subject.enType VI Secretion Systems
dc.title.enBiogenesis and structure of a type VI secretion baseplate.
dc.title.alternativeNat Microbiolen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1038/s41564-018-0260-1en_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologieen_US
dc.identifier.pubmed30323254en_US
bordeaux.journalNature Microbiologyen_US
bordeaux.page1404-1416en_US
bordeaux.volume3en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.issue12en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcepubmed
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exportfalse
workflow.import.sourcepubmed
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Nature%20Microbiology&rft.date=2018-12-01&rft.volume=3&rft.issue=12&rft.spage=1404-1416&rft.epage=1404-1416&rft.eissn=2058-5276&rft.issn=2058-5276&rft.au=CHERRAK,%20Yassine&RAPISARDA,%20Chiara&PELLARIN,%20Riccardo&BOUVIER,%20Guillaume&BARDIAUX,%20Benjamin&rft.genre=article


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