Control of membrane barrier during bacterial type-III protein secretion

Svenja Hüsing, Manuel Halte, Ulf Look, Alina Guse, Eric J. C. Gálvez, Emmanuelle Charpentier, David F. Blair, Marc Erhardt () and Thibaud T. Renault ()
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Svenja Hüsing: Humboldt-Universität zu Berlin
Manuel Halte: Humboldt-Universität zu Berlin
Ulf Look: Humboldt-Universität zu Berlin
Alina Guse: Humboldt-Universität zu Berlin
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
Thibaud T. Renault: Humboldt-Universität zu Berlin

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: 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.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24226-1

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DOI: 10.1038/s41467-021-24226-1

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