Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin.
| dc.rights.license | open | en_US |
| dc.contributor.author | JURĖNAS, Dukas | |
| hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
| dc.contributor.author | ROSA, Leonardo Talachia | |
| dc.contributor.author | REY, Martial | |
| dc.contributor.author | CHAMOT-ROOKE, Julia | |
| hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
| dc.contributor.author | FRONZES, Rémi | |
| dc.contributor.author | CASCALES, Eric | |
| dc.date.accessioned | 2024-10-07T10:01:34Z | |
| dc.date.available | 2024-10-07T10:01:34Z | |
| dc.date.issued | 2021-12-01 | |
| dc.identifier.issn | 2041-1723 | en_US |
| dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/202280 | |
| dc.description.abstractEn | Bacteria have evolved toxins to outcompete other bacteria or to hijack host cell pathways. One broad family of bacterial polymorphic toxins gathers multidomain proteins with a modular organization, comprising a C-terminal toxin domain fused to a N-terminal domain that adapts to the delivery apparatus. Polymorphic toxins include bacteriocins, contact-dependent growth inhibition systems, and specialized Hcp, VgrG, PAAR or Rhs Type VI secretion (T6SS) components. We recently described and characterized Tre23, a toxin domain fused to a T6SS-associated Rhs protein in Photorhabdus laumondii, Rhs1. Here, we show that Rhs1 forms a complex with the T6SS spike protein VgrG and the EagR chaperone. Using truncation derivatives and cross-linking mass spectrometry, we demonstrate that VgrG-EagR-Rhs1 complex formation requires the VgrG C-terminal β-helix and the Rhs1 N-terminal region. We then report the cryo-electron-microscopy structure of the Rhs1-EagR complex, demonstrating that the Rhs1 central region forms a β-barrel cage-like structure that encapsulates the C-terminal toxin domain, and provide evidence for processing of the Rhs1 protein through aspartyl autoproteolysis. We propose a model for Rhs1 loading on the T6SS, transport and delivery into the target cell. | |
| dc.language.iso | EN | en_US |
| dc.rights | Attribution 3.0 United States | * |
| dc.rights.uri | http://creativecommons.org/licenses/by/3.0/us/ | * |
| dc.subject.en | Adaptation | |
| dc.subject.en | Physiological | |
| dc.subject.en | Bacterial Proteins | |
| dc.subject.en | Bacterial Toxins | |
| dc.subject.en | Bacteriocins | |
| dc.subject.en | Contact Inhibition | |
| dc.subject.en | Cryoelectron Microscopy | |
| dc.subject.en | Mass Spectrometry | |
| dc.subject.en | Models | |
| dc.subject.en | Molecular | |
| dc.subject.en | Photorhabdus | |
| dc.subject.en | Type VI Secretion Systems | |
| dc.title.en | Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin. | |
| dc.title.alternative | Nat Commun | en_US |
| dc.type | Article de revue | en_US |
| dc.identifier.doi | 10.1038/s41467-021-27388-0 | en_US |
| dc.subject.hal | Sciences du Vivant [q-bio]/Microbiologie et Parasitologie | en_US |
| dc.identifier.pubmed | 34853317 | en_US |
| bordeaux.journal | Nature Communications | en_US |
| bordeaux.page | 6998 | en_US |
| bordeaux.volume | 12 | 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 | pubmed | |
| hal.popular | non | en_US |
| hal.audience | Internationale | en_US |
| hal.export | false | |
| workflow.import.source | pubmed | |
| 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=2021-12-01&rft.volume=12&rft.issue=1&rft.spage=6998&rft.epage=6998&rft.eissn=2041-1723&rft.issn=2041-1723&rft.au=JUR%C4%96NAS,%20Dukas&ROSA,%20Leonardo%20Talachia&REY,%20Martial&CHAMOT-ROOKE,%20Julia&FRONZES,%20R%C3%A9mi&rft.genre=article |
