![]() ![]() Key Words: Proton motive force, Sodium motive force, Energy transduction. This website requires cookies, and the limited processing of your personal data in order to function. The concept of proton motive force was proposed by Peter Mitchell in the 1960s, for which he was awarded the Nobel Prize in 1978. The rest of the successive unfolding/translocation process of the substrates is driven by proton motive force. Bacterial flagella are filamentous organelles that drive cell locomotion. Therefore, even anaerobic bacteria have ATP synthases to create a proton motive force to power activities like movement of flagella or ion transport. 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. Furthermore, proton motive force was essential for the export process. The export apparatus consists of a transmembrane PMF-driven export gate and a cytoplasmic ATPase complex composed of FliH, FliI and FliJ. 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. For self-assembly of the bacterial flagellum, a specific protein export apparatus utilizes ATP and proton motive force (PMF) as the energy source to transport component proteins to the distal growing end. A fliH fliI double null mutant was weakly motile. Here we report that flagellar proteins of Salmonella enterica serovar Typhimurium are exported even in the absence of FliI. The FliI ATPase is required for this export, and its ATPase activity is regulated by FliH however, it is unclear how the chemical energy derived from ATP hydrolysis is used for the export process. For construction of the bacterial flagellum responsible for motility, most of the components are exported by the flagellar protein export apparatus. ![]() Translocation of many soluble proteins across cell membranes occurs in an ATPase-driven manner. ![]()
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