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

Autor: Wimmi S; Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany., Balinovic A; Department of Systems and Synthetic Microbiology, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.; SYNMIKRO, Center for Synthetic Microbiology, Marburg, Germany.; Department of Physics, Carnegie Mellon University, Pittsburgh, PA, USA.; Institute for Microbiology and Biotechnology, Rheinische Friedrich-Wilhelms-Universität Bonn, Bonn, Germany., Brianceau C; Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany., Pintor K; Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany., Vielhauer J; Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany., Turkowyd B; Department of Systems and Synthetic Microbiology, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.; SYNMIKRO, Center for Synthetic Microbiology, Marburg, Germany.; Department of Physics, Carnegie Mellon University, Pittsburgh, PA, USA.; Institute for Microbiology and Biotechnology, Rheinische Friedrich-Wilhelms-Universität Bonn, Bonn, Germany., Helbig C; Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany., Fleck M; Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany., Langenfeld K; Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany., Kahnt J; Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.; Mass Spectrometry and Proteomics Facility, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany., Glatter T; Mass Spectrometry and Proteomics Facility, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany., Endesfelder U; Department of Systems and Synthetic Microbiology, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany. endesfelder@uni-bonn.de.; SYNMIKRO, Center for Synthetic Microbiology, Marburg, Germany. endesfelder@uni-bonn.de.; Department of Physics, Carnegie Mellon University, Pittsburgh, PA, USA. endesfelder@uni-bonn.de.; Institute for Microbiology and Biotechnology, Rheinische Friedrich-Wilhelms-Universität Bonn, Bonn, Germany. endesfelder@uni-bonn.de., Diepold A; Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany. andreas.diepold@mpi-marburg.mpg.de.; SYNMIKRO, Center for Synthetic Microbiology, Marburg, Germany. andreas.diepold@mpi-marburg.mpg.de.
Jazyk: angličtina
Zdroj: Nature microbiology [Nat Microbiol] 2024 Jan; Vol. 9 (1), pp. 185-199. Date of Electronic Publication: 2024 Jan 03.
DOI: 10.1038/s41564-023-01545-1
Abstrakt: 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.
(© 2024. The Author(s).)
Databáze: MEDLINE
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