Diverse roles of TssA-like proteins in the assembly of bacterial type VI secretion systems.

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Version: Final published version
License: CC BY 4.0
Serval ID
serval:BIB_CC696DD8885A
Type
Article: article from journal or magazin.
Collection
Publications
Title
Diverse roles of TssA-like proteins in the assembly of bacterial type VI secretion systems.
Journal
The EMBO journal
Author(s)
Schneider J.P., Nazarov S., Adaixo R., Liuzzo M., Ringel P.D., Stahlberg H., Basler M.
ISSN
1460-2075 (Electronic)
ISSN-L
0261-4189
Publication state
Published
Issued date
16/09/2019
Peer-reviewed
Oui
Volume
38
Number
18
Pages
e100825
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Abstract
Protein translocation by the bacterial type VI secretion system (T6SS) is driven by a rapid contraction of a sheath assembled around a tube with associated effectors. Here, we show that TssA-like or TagA-like proteins with a conserved N-terminal domain and varying C-terminal domains can be grouped into at least three distinct classes based on their role in sheath assembly. The proteins of the first class increase speed and frequency of sheath assembly and form a stable dodecamer at the distal end of a polymerizing sheath. The proteins of the second class localize to the cell membrane and block sheath polymerization upon extension across the cell. This prevents excessive sheath polymerization and bending, which may result in sheath destabilization and detachment from its membrane anchor and thus result in failed secretion. The third class of these proteins localizes to the baseplate and is required for initiation of sheath assembly. Our work shows that while various proteins share a conserved N-terminal domain, their roles in T6SS biogenesis are fundamentally different.
Keywords
Bacterial Proteins/chemistry, Bacterial Proteins/metabolism, Cell Membrane/metabolism, Gram-Negative Bacteria/metabolism, Lipoproteins/chemistry, Lipoproteins/metabolism, Models, Molecular, Protein Conformation, Protein Domains, Type VI Secretion Systems/metabolism, ImpA_N domain proteins, protein localization, protein-protein interactions, sheath assembly, type VI secretion system
Pubmed
Web of science
Open Access
Yes
Create date
09/06/2023 16:02
Last modification date
22/01/2024 8:36
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