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• W1901472965 endingPage "e1005545" @default.
• W1901472965 startingPage "e1005545" @default.
• W1901472965 abstract "The Type VI secretion system (T6SS) is a widespread weapon dedicated to the delivery of toxin proteins into eukaryotic and prokaryotic cells. The 13 T6SS subunits assemble a cytoplasmic contractile structure anchored to the cell envelope by a membrane-spanning complex. This structure is evolutionarily, structurally and functionally related to the tail of contractile bacteriophages. In bacteriophages, the tail assembles onto a protein complex, referred to as the baseplate, that not only serves as a platform during assembly of the tube and sheath, but also triggers the contraction of the sheath. Although progress has been made in understanding T6SS assembly and function, the composition of the T6SS baseplate remains mostly unknown. Here, we report that six T6SS proteins–TssA, TssE, TssF, TssG, TssK and VgrG–are required for proper assembly of the T6SS tail tube, and a complex between VgrG, TssE,-F and-G could be isolated. In addition, we demonstrate that TssF and TssG share limited sequence homologies with known phage components, and we report the interaction network between these subunits and other baseplate and tail components. In agreement with the baseplate being the assembly platform for the tail, fluorescence microscopy analyses of functional GFP-TssF and TssK-GFP fusion proteins show that these proteins assemble stable and static clusters on which the sheath polymerizes. Finally, we show that recruitment of the baseplate to the apparatus requires initial positioning of the membrane complex and contacts between TssG and the inner membrane TssM protein." @default.
• W1901472965 created "2016-06-24" @default.
• W1901472965 creator A5016978758 @default.
• W1901472965 creator A5018842385 @default.
• W1901472965 creator A5055016134 @default.
• W1901472965 creator A5070115867 @default.
• W1901472965 creator A5087094018 @default.
• W1901472965 date "2015-10-13" @default.
• W1901472965 modified "2023-10-10" @default.
• W1901472965 title "The Type VI Secretion TssEFGK-VgrG Phage-Like Baseplate Is Recruited to the TssJLM Membrane Complex via Multiple Contacts and Serves As Assembly Platform for Tail Tube/Sheath Polymerization" @default.
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• W1901472965 doi "https://doi.org/10.1371/journal.pgen.1005545" @default.
• W1901472965 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4604203" @default.
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• W1901472965 hasPublicationYear "2015" @default.
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