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Article Dans Une Revue Nucleic Acids Research Année : 2022

Salmonella antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of EF-Tu P-loop

Résumé

Abstract Rearrangement hot spot (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, TreTu, 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 Tu (EF-Tu). This modification is specifically placed on the side chain of the conserved D21 residue located on the P-loop of the EF-Tu G-domain. Finally, we demonstrate that the TriTu immunity protein neutralizes TreTu activity by acting like a lid that closes the catalytic site and traps the NAD+.
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Origine : Publication financée par une institution
Licence : CC BY NC - Paternité - Pas d'utilisation commerciale

Dates et versions

hal-04009485 , version 1 (23-03-2023)

Licence

Paternité - Pas d'utilisation commerciale

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Dukas Jurėnas, Martial Rey, Deborah Byrne, Julia Chamot-Rooke, Laurent Terradot, et al.. Salmonella antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of EF-Tu P-loop. Nucleic Acids Research, 2022, Methods in Molecular Biology, 50 (22), pp.13114-13127. ⟨10.1093/nar/gkac1162⟩. ⟨hal-04009485⟩
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