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dc.rights.licenseopenen_US
dc.contributor.authorTASSINARI, Matteo
dc.contributor.authorDOAN, Thierry
dc.contributor.authorBELLINZONI, Marco
dc.contributor.authorCHABALIER, Maïalene
dc.contributor.authorBEN-ASSAYA, Mathilde
dc.contributor.authorMARTINEZ, Mariano
dc.contributor.authorGADAY, Quentin
dc.contributor.authorALZARI, Pedro
dc.contributor.authorCASCALES, Eric
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorFRONZES, Rémi
dc.contributor.authorGUBELLINI, Francesca
dc.date.accessioned2023-05-15T07:15:30Z
dc.date.available2023-05-15T07:15:30Z
dc.date.issued2022-09-28
dc.identifier.issn2161-2129en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/182103
dc.description.abstractEnType VIIb secretion systems (T7SSb) were recently proposed to mediate different aspects of Firmicutes physiology, including bacterial pathogenicity and competition. However, their architecture and mechanism of action remain largely obscure. Here, we present a detailed analysis of the T7SSb-mediated bacterial competition in Bacillus subtilis, using the effector YxiD as a model for the LXG secreted toxins. By systematically investigating protein-protein interactions, we reveal that the membrane subunit YukC contacts all T7SSb components, including the WXG100 substrate YukE and the LXG effector YxiD. YukC's crystal structure shows unique features, suggesting an intrinsic flexibility that is required for T7SSb antibacterial activity. Overall, our results shed light on the role and molecular organization of the T7SSb and demonstrate the potential of B. subtilis as a model system for extensive structure-function studies of these secretion machineries. IMPORTANCE Type VII secretion systems mediate protein extrusion from Gram-positive bacteria and are classified as T7SSa and T7SSb in Actinobacteria and in Firmicutes, respectively. Despite the genetic divergence of T7SSa and T7SSb, the high degree of structural similarity of their WXG100 substrates suggests similar secretion mechanisms. Recent advances revealed the structures of several T7SSa cytoplasmic membrane complexes, but the molecular mechanism of secretion and the T7SSb architecture remain obscure. Here, we provide hints on the organization of T7SSb in B. subtilis and a highresolution structure of its central pseudokinase subunit, opening new perspectives for the understanding of the T7SSb secretion mechanism by using B. subtilis as an amenable bacterial model.
dc.language.isoENen_US
dc.rights.urihttp://creativecommons.org/licenses/by/
dc.subject.entype VIIb secretion system
dc.subject.enBacillus subtilis
dc.subject.enbacterial competition
dc.subject.enpseudokinase
dc.subject.encrystallographic structure
dc.subject.enbacterial two-hybrid assay
dc.subject.eninteraction network
dc.subject.enprotein complexes
dc.subject.enpseudokinases
dc.subject.ensecretion systems
dc.subject.enstructural biology
dc.title.enThe Antibacterial Type VII Secretion System of Bacillus subtilis: Structure and Interactions of the Pseudokinase YukC/EssB
dc.typeArticle de revueen_US
dc.identifier.doi10.1128/mbio.00134-22en_US
dc.subject.halSciences du Vivant [q-bio]en_US
bordeaux.journalmBioen_US
bordeaux.pagee0013422en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcehal
hal.identifierpasteur-03790349
hal.version1
hal.exportfalse
workflow.import.sourcehal
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=mBio&rft.date=2022-09-28&rft.spage=e0013422&rft.epage=e0013422&rft.eissn=2161-2129&rft.issn=2161-2129&rft.au=TASSINARI,%20Matteo&DOAN,%20Thierry&BELLINZONI,%20Marco&CHABALIER,%20Ma%C3%AFalene&BEN-ASSAYA,%20Mathilde&rft.genre=article


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