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• W2062892191 endingPage "488" @default.
• W2062892191 startingPage "485" @default.
• W2062892191 abstract "Bacterial flagella contain a secretion apparatus related to the type III secretion system used by many pathogens to transfer effector proteins into host cells. It is generally assumed that the ATPase FliI provides energy for transport, but two reports argue against this view. Both groups find that flagellar secretion occurs even in the absence of the ATPase, and that the energy required derives from the proton motive force. Bacterial flagella contain a secretion apparatus that is related to the type III secretion system used by many pathogens to transfer effector proteins into host cells. It has been thought that the ATPase, FliL provides the energy for transport. This is one of two papers that argue against this widely held view and show that flagellar secretion can occur even in the absence of the ATPase and is instead driven by the proton motive force. Translocation of many soluble proteins across cell membranes occurs in an ATPase-driven manner. For construction of the bacterial flagellum responsible for motility, most of the components are exported by the flagellar protein export apparatus1,2. The FliI ATPase is required for this export3, and its ATPase activity is regulated by FliH4; however, it is unclear how the chemical energy derived from ATP hydrolysis is used for the export process. Here we report that flagellar proteins of Salmonella enterica serovar Typhimurium are exported even in the absence of FliI. A fliH fliI double null mutant was weakly motile. Certain mutations in FlhA or FlhB, which form the core of the export gate, substantially improved protein export and motility of the double null mutant. Furthermore, proton motive force was essential for the export process. These results suggest that the FliH–FliI complex facilitates only the initial entry of export substrates into the gate, with the energy of ATP hydrolysis being used to disassemble and release the FliH–FliI complex from the protein about to be exported. The rest of the successive unfolding/translocation process of the substrates is driven by proton motive force." @default.
• W2062892191 created "2016-06-24" @default.
• W2062892191 creator A5025152584 @default.
• W2062892191 creator A5078668392 @default.
• W2062892191 date "2008-01-01" @default.
• W2062892191 modified "2023-10-06" @default.
• W2062892191 title "Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export" @default.
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• W2062892191 doi "https://doi.org/10.1038/nature06449" @default.
• W2062892191 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18216858" @default.
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