Structural basis for synthase activation and cellulose modification in the E. coli Type II Bcs secretion system
| dc.rights.license | open | en_US |
| hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
| dc.contributor.author | ANSO, Itxaso | |
| hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
| dc.contributor.author | ZOUHIR, Samira | |
| hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
| dc.contributor.author | SANA, Thibault Gery | |
| dc.contributor.author | KRASTEVA, Petya Violinova | |
| dc.date.accessioned | 2025-02-14T11:10:01Z | |
| dc.date.available | 2025-02-14T11:10:01Z | |
| dc.date.issued | 2024-10-11 | |
| dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/204895 | |
| dc.description.abstractEn | Bacterial cellulosic polymers constitute a prevalent class of biofilm matrix exopolysaccharides that are synthesized by several types of bacterial cellulose secretion (Bcs) systems, which include conserved cyclic diguanylate (c-di-GMP)-dependent cellulose synthase modules together with diverse accessory subunits. In E. coli, the biogenesis of phosphoethanolamine (pEtN)-modified cellulose relies on the BcsRQABEFG macrocomplex, encompassing innermembrane and cytosolic subunits, and an outer membrane porin, BcsC. Here, we use cryogenic electron microscopy to shed light on the molecular mechanisms of BcsA-dependent recruitment and stabilization of a trimeric BcsG pEtN-transferase for polymer modification, and a dimeric BcsFdependent recruitment of an otherwise cytosolic BcsE2R2Q2 regulatory complex. We further demonstrate that BcsE, a secondary c di-GMP sensor, can remain dinucleotide-bound and retain the essential for-secretion BcsRQ partners onto the synthase even in the absence of direct c-di-GMP-synthase complexation, likely lowering the threshold for c-di-GMP-dependent synthase activation. Such activation-by-proxy mechanism could allow Bcs secretion system activity even in the absence of substantial intracellular c-di-GMP increase, and is reminiscent of other widespread synthase-dependent polysaccharide secretion systems where dinucleotide sensing and/or synthase stabilization are carried out by key co-polymerase subunits. | |
| dc.description.sponsorship | Mécanismes de la Sécrétion de Cellulose Bactérienne dans les Interactions avec les Plantes Hôtes - ANR-23-CE11-0015 | en_US |
| dc.description.sponsorship | Structure et régulation des systèmes de sécrétion d'exopolysaccharides dans les biofilms bactériens - ANR-24-ERCC-0002 | en_US |
| dc.language.iso | EN | en_US |
| dc.rights | Attribution-NonCommercial-NoDerivs 3.0 United States | * |
| dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/us/ | * |
| dc.title.en | Structural basis for synthase activation and cellulose modification in the E. coli Type II Bcs secretion system | |
| dc.type | Article de revue | en_US |
| dc.identifier.doi | 10.1038/s41467-024-53113-8 | en_US |
| dc.subject.hal | Chimie/Matériaux | en_US |
| dc.identifier.pubmed | 39394223 | en_US |
| bordeaux.journal | Nature Communications | en_US |
| bordeaux.page | 8799 | en_US |
| bordeaux.volume | 15 | en_US |
| bordeaux.hal.laboratories | CBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248 | en_US |
| bordeaux.issue | 1 | en_US |
| bordeaux.institution | Université de Bordeaux | en_US |
| bordeaux.institution | Bordeaux INP | en_US |
| bordeaux.institution | CNRS | en_US |
| bordeaux.peerReviewed | oui | en_US |
| bordeaux.inpress | non | en_US |
| hal.popular | non | en_US |
| hal.audience | Internationale | en_US |
| hal.export | false | |
| dc.rights.cc | CC BY-NC-ND | en_US |
| bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Nature%20Communications&rft.date=2024-10-11&rft.volume=15&rft.issue=1&rft.spage=8799&rft.epage=8799&rft.au=ANSO,%20Itxaso&ZOUHIR,%20Samira&SANA,%20Thibault%20Gery&KRASTEVA,%20Petya%20Violinova&rft.genre=article |