The type VI secretion system sheath assembles at the end distal from the membrane anchor.
Détails
ID Serval
serval:BIB_EB1AB628FE85
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
The type VI secretion system sheath assembles at the end distal from the membrane anchor.
Périodique
Nature communications
ISSN
2041-1723 (Electronic)
ISSN-L
2041-1723
Statut éditorial
Publié
Date de publication
13/07/2017
Peer-reviewed
Oui
Volume
8
Pages
16088
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: epublish
Publication Status: epublish
Résumé
The bacterial Type VI secretion system (T6SS) delivers proteins into target cells using fast contraction of a long sheath anchored to the cell envelope and wrapped around an inner Hcp tube associated with the secreted proteins. Mechanisms of sheath assembly and length regulation are unclear. Here we study these processes using spheroplasts formed from ampicillin-treated Vibrio cholerae. We show that spheroplasts secrete Hcp and deliver T6SS substrates into neighbouring cells. Imaging of sheath dynamics shows that the sheath length correlates with the diameter of spheroplasts and may reach up to several micrometres. Analysis of sheath assembly after partial photobleaching shows that subunits are exclusively added to the sheath at the end that is distal from the baseplate and cell envelope attachment. We suggest that this mode of assembly is likely common for all phage-like contractile nanomachines, because of the conservation of the structures and connectivity of sheath subunits.
Mots-clé
Ampicillin, Cell Size, Polymerization, Type VI Secretion Systems/metabolism, Vibrio cholerae/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
22/07/2024 16:10
Dernière modification de la notice
27/07/2024 7:01