PXD028652

PXD028652 is an original dataset announced via ProteomeXchange.

Title	Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin
Description	Bacteria have evolved effectors or toxins to outcompete other bacteria or to hijack host cell pathways. One broad family of bacterial polymorphic toxins regroups multidomain proteins with a modular organization, that comprise a C-terminal toxin domain fused to a N-terminal domain that adapt 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. Here, we show that the Rhs polymorphic toxin forms a complex with the T6SS spike protein VgrG and a cognate chaperone EagR. Using truncation derivatives and cross-linking mass spectrometry, we demonstrate that VgrG-EagR-Rhs complex formation requires the VgrG C-terminal β-helix and the Rhs Nterminal prePAAR and PAAR domains. We then report the cryo-electron-microscopy structure of the Rhs-EagR complex, demonstrating that the Rhs central region forms a β-barrel cage-like structure that encapsulates the C-terminal toxin domain, and provide evidence for processing of the Rhs protein through aspartyl autoproteolysis. We propose a model for Rhs loading on the T6SS, transport and delivery into the target cell.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:30:36.263.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Martial Rey
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562; scientific name: Bacteria; NCBI TaxID: NCBITaxon:2;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2021-09-20 06:58:19	ID requested
1	2021-11-30 06:45:30	announced
2	2023-04-11 06:23:32	announced	2023-04-11: Updated project metadata.
⏵ 3	2024-10-22 05:30:37	announced	2024-10-22: Updated project metadata.

10.1038/s41467-021-27388-0;

Jur, ė, nas D, Rosa LT, Rey M, Chamot-Rooke J, Fronzes R, Cascales E, Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin. Nat Commun, 12(1):6998(2021) [pubmed]

submitter keyword: Re-arrangement hot spot, spike, cross-linking, polymorphic toxin, β-roll, chaperone, autocleavage, VgrG, architecture

Julia Chamot-Rooke
contact affiliation	Mass Spectrometry for Biology Unit, CNRS USR2000, Institut Pasteur, CNRS, 28 rue du Dr Roux, Paris 75015, France.
contact email	julia.chamot-rooke@pasteur.fr
lab head
Martial Rey
contact affiliation	CNRS, Pasteur
contact email	martial.rey@pasteur.fr
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2021/11/PXD028652

PRIDE project URI

• PRIDE
  1. PXD028652
     1. Label: PRIDE project
     2. Name: Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin