Insights into the structure and assembly of a bacterial cellulose secretion system
| dc.rights.license | open | en_US |
| dc.contributor.author | KRASTEVA, Petya Violinova | |
| dc.contributor.author | BERNAL-BAYARD, Joaquin | |
| dc.contributor.author | TRAVIER, Laetitia | |
| dc.contributor.author | MARTIN, Fernando Ariel | |
| dc.contributor.author | KAMINSKI, Pierre-Alexandre | |
| dc.contributor.author | KARIMOVA, Gouzel | |
| hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
| dc.contributor.author | FRONZES, Rémi | |
| dc.contributor.author | GHIGO, Jean-Marc | |
| dc.date.accessioned | 2023-06-28T09:41:36Z | |
| dc.date.available | 2023-06-28T09:41:36Z | |
| dc.date.issued | 2017-12-12 | |
| dc.identifier.issn | 2041-1723 | en_US |
| dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/183213 | |
| dc.description.abstractEn | Secreted exopolysaccharides present important determinants for bacterial biofilm formation, survival, and virulence. Cellulose secretion typically requires the concerted action of a c-di-GMP-responsive inner membrane synthase (BcsA), an accessory membrane-anchored protein (BcsB), and several additional Bcs components. Although the BcsAB catalytic duo has been studied in great detail, its interplay with co-expressed subunits remains enigmatic. Here we show that E. coli Bcs proteins partake in a complex protein interaction network. Electron microscopy reveals a stable, megadalton-sized macromolecular assembly, which encompasses most of the inner membrane and cytosolic Bcs components and features a previously unobserved asymmetric architecture. Heterologous reconstitution and mutational analyses point toward a structure-function model, where accessory proteins regulate secretion by affecting both the assembly and stability of the system. Altogether, these results lay the foundation for more comprehensive models of synthase-dependent exopolysaccharide secretion in biofilms and add a sophisticated secretory nanomachine to the diverse bacterial arsenal for virulence and adaptation. | |
| dc.description.sponsorship | Integrative Biology of Emerging Infectious Diseases | en_US |
| dc.language.iso | EN | en_US |
| dc.rights.uri | http://creativecommons.org/licenses/by/ | |
| dc.subject.en | Bacterial secretion | |
| dc.subject.en | Bacterial structural biology | |
| dc.subject.en | Biofilms | |
| dc.subject.en | Electron microscopy | |
| dc.title.en | Insights into the structure and assembly of a bacterial cellulose secretion system | |
| dc.type | Article de revue | en_US |
| dc.identifier.doi | 10.1038/s41467-017-01523-2 | en_US |
| dc.subject.hal | Sciences du Vivant [q-bio] | en_US |
| dc.subject.hal | Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire | en_US |
| dc.description.sponsorshipEurope | Molecular and Structural Biology of Bacterial Transformation | en_US |
| bordeaux.journal | Nature Communications | en_US |
| bordeaux.page | 2065 | en_US |
| bordeaux.volume | 8 | en_US |
| bordeaux.hal.laboratories | MFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234 | en_US |
| bordeaux.issue | 1 | en_US |
| bordeaux.institution | CNRS | en_US |
| bordeaux.peerReviewed | oui | en_US |
| bordeaux.inpress | non | en_US |
| bordeaux.import.source | hal | |
| hal.identifier | pasteur-01688314 | |
| hal.version | 1 | |
| hal.export | false | |
| workflow.import.source | hal | |
| dc.rights.cc | Pas de Licence CC | en_US |
| bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Nature%20Communications&rft.date=2017-12-12&rft.volume=8&rft.issue=1&rft.spage=2065&rft.epage=2065&rft.eissn=2041-1723&rft.issn=2041-1723&rft.au=KRASTEVA,%20Petya%20Violinova&BERNAL-BAYARD,%20Joaquin&TRAVIER,%20Laetitia&MARTIN,%20Fernando%20Ariel&KAMINSKI,%20Pierre-Alexandre&rft.genre=article |
