Author
Listed:
- Svenja Hüsing
(Humboldt-Universität zu Berlin
Max Planck Unit for the Science of Pathogens)
- Manuel Halte
(Humboldt-Universität zu Berlin)
- Ulf Look
(Humboldt-Universität zu Berlin
Max Planck Unit for the Science of Pathogens)
- Alina Guse
(Humboldt-Universität zu Berlin
Harvard University)
- Eric J. C. Gálvez
(Max Planck Unit for the Science of Pathogens)
- Emmanuelle Charpentier
(Max Planck Unit for the Science of Pathogens)
- David F. Blair
(University of Utah)
- Marc Erhardt
(Humboldt-Universität zu Berlin
Max Planck Unit for the Science of Pathogens)
- Thibaud T. Renault
(Humboldt-Universität zu Berlin
Max Planck Unit for the Science of Pathogens
Université de Bordeaux
Université de Bordeaux)
Abstract
Type-III secretion systems (T3SSs) of the bacterial flagellum and the evolutionarily related injectisome are capable of translocating proteins with a remarkable speed of several thousand amino acids per second. Here, we investigate how T3SSs are able to transport proteins at such a high rate while preventing the leakage of small molecules. Our mutational and evolutionary analyses demonstrate that an ensemble of conserved methionine residues at the cytoplasmic side of the T3SS channel create a deformable gasket (M-gasket) around fast-moving substrates undergoing export. The unique physicochemical features of the M-gasket are crucial to preserve the membrane barrier, to accommodate local conformational changes during active secretion, and to maintain stability of the secretion pore in cooperation with a plug domain (R-plug) and a network of salt-bridges. The conservation of the M-gasket, R-plug, and salt-bridge network suggests a universal mechanism by which the membrane integrity is maintained during high-speed protein translocation in all T3SSs.
Suggested Citation
Svenja Hüsing & Manuel Halte & Ulf Look & Alina Guse & Eric J. C. Gálvez & Emmanuelle Charpentier & David F. Blair & Marc Erhardt & Thibaud T. Renault, 2021.
"Control of membrane barrier during bacterial type-III protein secretion,"
Nature Communications, Nature, vol. 12(1), pages 1-12, December.
Handle:
RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24226-1
DOI: 10.1038/s41467-021-24226-1
Download full text from publisher
Corrections
All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24226-1. See general information about how to correct material in RePEc.
If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.
We have no bibliographic references for this item. You can help adding them by using this form .
If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.
For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .
Please note that corrections may take a couple of weeks to filter through
the various RePEc services.