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  Cytosolic sorting platform complexes shuttle type III secretion system effectors to the injectisome in Yersinia enterocolitica

Wimmi, S., Balinovic, A., Brianceau, C. F., Pintor, K. L., Vielhauer, J., Turkowyd, B., et al. (2024). Cytosolic sorting platform complexes shuttle type III secretion system effectors to the injectisome in Yersinia enterocolitica. Nature Microbiology, 9, 185-199. doi:10.1038/s41564-023-01545-1.

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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-000E-1AA0-0 Versions-Permalink: https://hdl.handle.net/21.11116/0000-000F-482D-F
Genre: Zeitschriftenartikel

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externe Referenz:
https://doi.org/10.1038/s41564-023-01545-1 (Verlagsversion)
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Verlagsversion
OA-Status:
Gold

Urheber

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 Urheber:
Wimmi, Stephan1, Autor           
Balinovic, Alexander2, Autor           
Brianceau, Corentin Florian1, Autor           
Pintor, Katherine Lapis1, Autor           
Vielhauer, Jan1, Autor           
Turkowyd, Bartosz3, Autor           
Helbig, Carlos1, Autor           
Fleck, Moritz1, Autor           
Langenfeld, Katja1, Autor           
Kahnt, Jörg4, Autor           
Glatter, Timo4, Autor                 
Endesfelder, Ulrike3, 5, Autor           
Diepold, Andreas1, Autor                 
Affiliations:
1Research Group Bacterial Secretion Systems, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266306              
2Microbial Networks, Department of Systems and Synthetic Microbiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266309              
3Department of Systems and Synthetic Microbiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266288              
4Core Facility Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266266              
5external, ou_persistent22              

Inhalt

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Schlagwörter: -
 Zusammenfassung: Bacteria use type III secretion injectisomes to inject effector proteins into eukaryotic target cells. Recruitment of effectors to the machinery and the resulting export hierarchy involve the sorting platform. These conserved proteins form pod structures at the cytosolic interface of the injectisome but are also mobile in the cytosol. Photoactivated localization microscopy in Yersinia enterocolitica revealed a direct interaction of the sorting platform proteins SctQ and SctL with effectors in the cytosol of live bacteria. These proteins form larger cytosolic protein complexes involving the ATPase SctN and the membrane connector SctK. The mobility and composition of these mobile pod structures are modulated in the presence of effectors and their chaperones, and upon initiation of secretion, which also increases the number of injectisomes from ~5 to ~18 per bacterium. Our quantitative data support an effector shuttling mechanism, in which sorting platform proteins bind to effectors in the cytosol and deliver the cargo to the export gate at the membrane-bound injectisome.

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Sprache(n): eng - English
 Datum: 2023-11-062024
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: URI: https://doi.org/10.1038/s41564-023-01545-1
Anderer: Wimmi2024
DOI: 10.1038/s41564-023-01545-1
 Art des Abschluß: -

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Projektinformation

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Projektname : -
Grant ID : -
Förderprogramm : -
Förderorganisation : Max Planck Society
Projektname : -
Grant ID : DI 1765/5-1
Förderprogramm : Foundation CELLEX
Förderorganisation : Max Planck Society
Projektname : -
Grant ID : PPP USA 2021-2023
Förderprogramm : -
Förderorganisation : German Research Foundation (DFG)
Projektname : -
Grant ID : -
Förderprogramm : -
Förderorganisation : Deutscher Akademischer Austausch Dienst (DAAD)
Projektname : -
Grant ID : -
Förderprogramm : -
Förderorganisation : Max Planck Institute for Terrestrial Microbiology, Marburg

Quelle 1

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Titel: Nature Microbiology
  Kurztitel : Nat. Microbiol.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: London, UK : Nature Publishing Group
Seiten: - Band / Heft: 9 Artikelnummer: - Start- / Endseite: 185 - 199 Identifikator: ISSN: 2058-5276
CoNE: https://pure.mpg.de/cone/journals/resource/2058-5276