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TitleDiverse roles of TssA-like proteins in the assembly of bacterial type VI secretion systems.
Journal, issue, pagesEMBO J, Vol. 38, Issue 18, Page e100825, Year 2019
Publish dateSep 16, 2019
AuthorsJohannes Paul Schneider / Sergey Nazarov / Ricardo Adaixo / Martina Liuzzo / Peter David Ringel / Henning Stahlberg / Marek Basler /
PubMed AbstractProtein 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 ...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.
External linksEMBO J / PubMed:31403721 / PubMed Central
MethodsEM (single particle)
Resolution3.9 Å
Structure data

4898

6riu

EMDB-4898: TssA protein from T6SS of Vibrio cholerae.
PDB-6riu: C-terminal domain of TssA protein from T6SS of Vibrio cholerae.
Method: EM (single particle) / Resolution: 3.9 Å

Source
  • vibrio cholerae (bacteria)
KeywordsTRANSPORT PROTEIN / T6SS / Vibrio / TssA / cap

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