Control of membrane barrier during bacterial type-III protein secretion.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
28 06 2021
28 06 2021
Historique:
received:
17
11
2020
accepted:
02
06
2021
entrez:
29
6
2021
pubmed:
30
6
2021
medline:
23
7
2021
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 34183670
doi: 10.1038/s41467-021-24226-1
pii: 10.1038/s41467-021-24226-1
pmc: PMC8239009
doi:
Substances chimiques
Bacterial Proteins
0
Carrier Proteins
0
Membrane Proteins
0
Type III Secretion Systems
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3999Références
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