Structures and roles of BcsD and partner scaffold proteins in proteobacterial cellulose secretion
2024
Sana, Thibault | Notopoulou, Areti | Puygrenier, Lucie | Decossas, Marion | Moreau, Sandra | Carlier, Aurélien | Krasteva, Petya | Chimie et Biologie des Membranes et des Nanoobjets (CBMN) ; Université de Bordeaux (UB)-École Nationale d'Ingénieurs des Travaux Agricoles - Bordeaux (ENITAB)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS) | Institut Européen de Chimie et Biologie (IECB) ; Université de Bordeaux (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS) | Laboratoire des Interactions Plantes Microbes Environnement (LIPME) ; Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) | Universiteit Gent = Ghent University = Université de Gand (UGENT) | This project received funding from the ERC Executive Agency under grant agreement 757507-BioMatrix-ERC-2017-StG (to P.V.K.) and was also supported by the IECB, the CNRS, a Universite de Bordeaux IDEX Junior Chair grant ExoPol (to P.V.K.) , and an ERASMUS+ Intern Traineeship Program (to A.N.); the work has also supported and has benefited from the IECB cryo-EM platform,
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Show more [+] Less [-]English. Cellulose 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.
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