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dc.rights.licenseopenen_US
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorSANA, Thibault Gery
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorNOTOPOULOU, Areti
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorPUYGRENIER, Lucie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorDECOSSAS, Marion
dc.contributor.authorMOREAU, Sandra
dc.contributor.authorCARLIER, Aurelien
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorKRASTEVA, Petya Violinova
dc.date.accessioned2025-02-11T14:39:02Z
dc.date.available2025-02-11T14:39:02Z
dc.date.issued2024-01-08
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/204796
dc.description.abstractEnCellulose is the world's most abundant biopolymer, and similar to its role as a cell wall component in plants, it is a prevalent constituent of the extracellular matrix in bacterial biofilms. Although bacterial cellulose (BC) was first described in the 19th century, it was only recently revealed that it is produced by several distinct types of Bcs secretion systems that feature multiple accessory subunits in addition to a catalytic BcsAB synthase tandem. We recently showed that crystalline cellulose secretion in the Gluconacetobacter genus (a-Proteobacteria) is driven by a supramolecular BcsH-BcsD scaffold-the "cortical belt"-which stabilizes the synthase nanoarrays through an unexpected inside -out mechanism for secretion system assembly. Interestingly, while bcsH is specific for Gluconacetobacter, bcsD homologs are widespread in Proteobacteria. Here, we examine BcsD homologs and their gene neighborhoods from several plant -colonizing b- and g-Proteobacteria proposed to secrete a variety of non -crystalline and/or chemically modified cellulosic polymers. We provide structural and mechanistic evidence that through different quaternary structure assemblies BcsD acts with proline-rich BcsH, BcsP, or BcsO partners across the proteobacterial clade to form synthase-interacting intracellular scaffolds that, in turn, determine the biofilm strength and architecture in species with strikingly different physiology and secreted biopolymers.
dc.language.isoENen_US
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/us/*
dc.subject.enBacterial biofilms
dc.subject.enBacterial cellulose
dc.subject.enC-di-GMP signaling
dc.subject.enMatrix exopolysaccharides
dc.subject.enSynthase-dependent systems
dc.title.enStructures and roles of BcsD and partner scaffold proteins in proteobacterial cellulose secretion
dc.typeArticle de revueen_US
dc.identifier.doi10.1016/j.cub.2023.11.057en_US
dc.subject.halChimie/Matériauxen_US
dc.identifier.pubmed38141614en_US
bordeaux.journalCurrent Biology - CBen_US
bordeaux.page106-116.e6en_US
bordeaux.volume34en_US
bordeaux.hal.laboratoriesCBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248en_US
bordeaux.issue1en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exportfalse
dc.rights.ccCC BY-NC-NDen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Current%20Biology%20-%20CB&rft.date=2024-01-08&rft.volume=34&rft.issue=1&rft.spage=106-116.e6&rft.epage=106-116.e6&rft.au=SANA,%20Thibault%20Gery&NOTOPOULOU,%20Areti&PUYGRENIER,%20Lucie&DECOSSAS,%20Marion&MOREAU,%20Sandra&rft.genre=article


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