Roles of H+-ATPase and proton motive force in ATP-dependent protein translocation in vitro.
Membrane vesicles from an Escherichia coli mutant with a deletion of the uncBC operon required ATP to translocate proteins, thus ruling out an essential role of F1F0-H+-ATPase in ATP-dependent protein translocation. Moreover, proteins could be translocated in the absence of proton motive force. At suboptimal ATP concentrations, D-lactate stimulated protein translocation, indicating that proton motive force, although insufficient to support translocation, could facilitate the process.
Chen
L L
LL
Tai
P C
PC
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D001426:Bacterial Proteins / Q000378:metabolism*; D001693:Biological Transport, Active; D002462:Cell Membrane / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007773:Lactates / Q000494:pharmacology; D019344:Lactic Acid; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D011522:Protons
D001426:Bacterial Proteins; D007773:Lactates; D011522:Protons; D019344:Lactic Acid; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases