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• W2894220510 abstract "The type VI secretion system (T6SS) is a multiprotein weapon used by bacteria to destroy competitor cells. The T6SS contractile sheath wraps an effector-loaded syringe that is injected into the target cell. This tail structure assembles onto the baseplate that is docked to the membrane complex. In enteroaggregative Escherichia coli, TssA plays a central role at each stage of the T6SS assembly pathway by stabilizing the baseplate and coordinating the polymerization of the tail. Here we adapted an assay based on APEX2-dependent biotinylation to identify the proximity partners of TssA in vivo. By using stage-blocking mutations, we define the temporal contacts of TssA during T6SS biogenesis. This proteomic mapping approach also revealed an additional partner of TssA, TagA. We show that TagA is a cytosolic protein tightly associated with the membrane. Analyses of sheath dynamics further demonstrate that TagA captures the distal end of the sheath to stop its polymerization and to maintain it under the extended conformation. The adaptation of APEX2-dependent proximity biotinylation for use in bacteria enables the identification of binding partners of TssA, which controls T6SS sheath assembly. This approach identifies TagA as a TssA partner that stops sheath polymerization and clamps the extended sheath to the membrane." @default.
• W2894220510 created "2018-10-05" @default.
• W2894220510 creator A5018842385 @default.
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• W2894220510 creator A5084564120 @default.
• W2894220510 date "2018-10-01" @default.
• W2894220510 modified "2023-10-13" @default.
• W2894220510 title "In vivo TssA proximity labelling during type VI secretion biogenesis reveals TagA as a protein that stops and holds the sheath" @default.
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• W2894220510 doi "https://doi.org/10.1038/s41564-018-0234-3" @default.
• W2894220510 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30275513" @default.
• W2894220510 hasPublicationYear "2018" @default.
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