主催: Japan Agency for Marine-Earth Science and Technology
共催: Toyo University, Japan Society for the Promotion of Science
p. 228-233
In alkaliphilic Bacillus, Na+-dependent pH homeostasis involves Na+/H+ antiport activities as well as Na+ re-entry routes. The MotPS flagellar stator proteins that are homologous to MotAB are required for the Na+-dependent motility of alkaliphilic B. pseudofirmus OF4. Purified and reconstituted MotPS support amiloride analogue-sensitive Na+ flux. Mutants lacking functional MotPS display no deficit in pH homeostasis in pH shift experiments conducted with sub-optimal added [Na+] in the absence of solutes whose uptake is coupled to Na+ re-entry. By contrast, a role was evident for the recently described NavBP (voltage-dependent) Na+ channel at sub-optimal [Na+]. NavBP mutants exhibit a significant loss of pH homeostasis capacity. NavBP has an additional role in chemotaxis; mutants in NavBP exhibited inverse chemotaxis as did the wild type alkaliphile when treated with the NavBP channel inhibitor nifedipine.