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PXD033100

PXD033100 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleSalmonella antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of EF-Tu P-loop
DescriptionRearrangement hot spots (Rhs) proteins are members of the broad family of polymorphic toxins. Polymorphic toxins are modular proteins composed of an N-terminal region that specifies their mode of secretion into the medium or into the target cell, a central delivery module and a C-terminal domain that has toxic activity. Here, we structurally and functionally characterize the C-terminal toxic domain of the antibacterial Rhsmain protein, which is delivered by the Type VI secretion system of Salmonella enterica Typhimurium. We show that this domain adopts an ADP-ribosyltransferase fold and inhibits protein synthesis by transferring an ADP-ribose group from NAD+ to the elongation factor EFTu. This modification is specifically placed on the sidechain of the conserved D21 residue located on the P-loop of the EF-Tu G-domain. Finally, we demonstrate that its cognate immunity protein neutralizes Rhsmain C-terminal toxin activity by acting like a lid that closes the catalytic site and traps the NAD+.
HostingRepositoryPRIDE
AnnounceDate2023-03-11
AnnouncementXMLSubmission_2023-03-11_03:48:10.076.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterMartialRey
SpeciesList scientific name: Escherichia coli; NCBI TaxID: 562; scientific name: Bacteria; NCBI TaxID: NCBITaxon:2; scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListadenosine diphosphoribosyl (ADP-ribosyl) modified residue
InstrumentQ Exactive HF; Orbitrap Fusion Lumos
Dataset History
RevisionDatetimeStatusChangeLog Entry
02022-04-08 01:25:35ID requested
12023-03-11 03:48:10announced
Publication List
Jur, ė, nas D, Rey M, Byrne D, Chamot-Rooke J, Terradot L, Cascales E, Salmonella antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of EF-Tu P-loop. Nucleic Acids Res, 50(22):13114-13127(2022) [pubmed]
Keyword List
submitter keyword: elongation factor, ADPribosylation, toxin, rearrangement hot spots,T6SS, P-loop, modification, translation
Contact List
JuliaChamot-Rooke
contact affiliationMass Spectrometry for Biology Unit, CNRS USR2000, Institut Pasteur, CNRS, 28 rue du Dr Roux, Paris 75015, France.
contact emailjulia.chamot-rooke@pasteur.fr
lab head
MartialRey
contact affiliationCNRS, Pasteur
contact emailmartial.rey@pasteur.fr
dataset submitter
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