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14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface
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2018 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 9, article id 3785Article in journal (Refereed) Published
Abstract [en]

Pseudomonas are a common cause of hospital-acquired infections that may be lethal. ADP-ribosyltransferase activities of Pseudomonas exotoxin-S and -T depend on 14-3-3 proteins inside the host cell. By binding in the 14-3-3 phosphopeptide binding groove, an amphipathic C-terminal helix of ExoS and ExoT has been thought to be crucial for their activation. However, crystal structures of the 14-3-3 beta: ExoS and -ExoT complexes presented here reveal an extensive hydrophobic interface that is sufficient for complex formation and toxin activation. We show that C-terminally truncated ExoS ADP-ribosyltransferase domain lacking the amphipathic binding motif is active when co-expressed with 14-3-3. Moreover, swapping the amphipathic C-terminus with a fragment from Vibrio Vis toxin creates a 14-3-3 independent toxin that ADP-ribosylates known ExoS targets. Finally, we show that 14-3-3 stabilizes ExoS against thermal aggregation. Together, this indicates that 14-3-3 proteins activate exotoxin ADP-ribosyltransferase domains by chaperoning their hydrophobic surfaces independently of the amphipathic C-terminal segment.

Place, publisher, year, edition, pages
Nature Publishing Group, 2018. Vol. 9, article id 3785
National Category
Cell and Molecular Biology Biochemistry and Molecular Biology
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URN: urn:nbn:se:umu:diva-152249DOI: 10.1038/s41467-018-06194-1ISI: 000444757900003PubMedID: 30224724OAI: oai:DiVA.org:umu-152249DiVA, id: diva2:1253312
Funder
Swedish Foundation for Strategic Research , SB12-0022Swedish Research Council, 2012-2802Swedish Research Council, 2015-4200Swedish Research Council, 2015-4603Wenner-Gren FoundationsAvailable from: 2018-10-04 Created: 2018-10-04 Last updated: 2018-10-04Bibliographically approved

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Lindberg, Mikael J.Caraballo, RemiElofsson, Mikael

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