English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  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.

Item is

Files

show Files

Locators

show
hide
Locator:
https://doi.org/10.1038/s41564-023-01545-1 (Publisher version)
Description:
Verlagsversion
OA-Status:
Gold

Creators

show
hide
 Creators:
Wimmi, Stephan1, Author           
Balinovic, Alexander2, Author           
Brianceau, Corentin Florian1, Author           
Pintor, Katherine Lapis1, Author           
Vielhauer, Jan1, Author           
Turkowyd, Bartosz3, Author           
Helbig, Carlos1, Author           
Fleck, Moritz1, Author           
Langenfeld, Katja1, Author           
Kahnt, Jörg4, Author           
Glatter, Timo4, Author                 
Endesfelder, Ulrike3, 5, Author           
Diepold, Andreas1, Author                 
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              

Content

show
hide
Free keywords: -
 Abstract: 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.

Details

show
hide
Language(s): eng - English
 Dates: 2023-11-062024
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show hide
Project name : -
Grant ID : -
Funding program : -
Funding organization : Max Planck Society
Project name : -
Grant ID : DI 1765/5-1
Funding program : Foundation CELLEX
Funding organization : Max Planck Society
Project name : -
Grant ID : PPP USA 2021-2023
Funding program : -
Funding organization : German Research Foundation (DFG)
Project name : -
Grant ID : -
Funding program : -
Funding organization : Deutscher Akademischer Austausch Dienst (DAAD)
Project name : -
Grant ID : -
Funding program : -
Funding organization : Max Planck Institute for Terrestrial Microbiology, Marburg

Source 1

show
hide
Title: Nature Microbiology
  Abbreviation : Nat. Microbiol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London, UK : Nature Publishing Group
Pages: - Volume / Issue: 9 Sequence Number: - Start / End Page: 185 - 199 Identifier: ISSN: 2058-5276
CoNE: https://pure.mpg.de/cone/journals/resource/2058-5276