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

Schneider, Johannes Paul and Nazarov, Sergey and Adaixo, Ricardo and Liuzzo, Martina and Ringel, Peter David and Stahlberg, Henning and Basler, Marek. (2019) Diverse roles of TssA-like proteins in the assembly of bacterial type VI secretion systems. The EMBO journal, 38. e100825.

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Official URL: https://edoc.unibas.ch/71708/

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Infection Biology > Infection Biology (Basler)
05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Stahlberg)
UniBasel Contributors:Stahlberg, Henning and Basler, Marek
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:EMBO Press
ISSN:0261-4189
e-ISSN:1460-2075
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
Identification Number:
Last Modified:29 Apr 2020 06:31
Deposited On:29 Apr 2020 06:31

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