Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export

Article

关键词: III SECRETION;    SALMONELLA-TYPHIMURIUM;    ESCHERICHIA-COLI;    CATALYTIC CYCLE;    COMPONENTS;    APPARATUS;    OLIGOMERIZATION;    SPECIFICITY;    SIMILARITY;    REGULATOR;   

DOI  :  10.1038/nature06449

来源: SCIE

【 摘 要 】

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 apparatus(1,2). The FliI ATPase is required for this export(3), and its ATPase activity is regulated by FliH(4); 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.

【 授权许可】

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