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

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In the environment, bacteria compete for privileged access to nutrients or to a particular niche. Bacteria have therefore evolved mechanisms to eliminate competitors. Among them, the Type VI secretion system (T6SS) is a contractile machine functionally comparable to a crossbow: an inner tube is wrapped by a contractile structure. Upon contraction of this outer sheath, the inner tube is propelled towards the target cell and delivers anti-bacterial effectors. The tubular structure assembles on a protein complex called the baseplate. Here we define the composition of the baseplate, demonstrating that it is composed of five subunits: TssE, TssF, TssG, TssK and VgrG. We further detail the role of the TssF and TssG proteins by defining their localizations and identifying their partners. We show that, in addition to TssE and VgrG that have been shown to share homologies with the bacteriophage gp25 and gp27-gp5 proteins, the TssF and TssG proteins also have homologies with bacteriophage components. Finally, we show that this baseplate is recruited to the TssJLM membrane complex prior to the assembly of the contractile tail structure. This study allows a better understanding of the early events of the assembly pathway of this molecular weapon.

Vyšlo v časopise: 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. PLoS Genet 11(10): e32767. doi:10.1371/journal.pgen.1005545
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1005545

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