Chen L L, Tai P C
J Bacteriol. 1986 Jul;167(1):389-92. doi: 10.1128/jb.167.1.389-392.1986.
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.
来自缺失uncBC操纵子的大肠杆菌突变体的膜囊泡需要ATP来转运蛋白质,从而排除了F1F0-H⁺-ATPase在ATP依赖性蛋白质转运中的关键作用。此外,在没有质子动力势的情况下蛋白质也可以转运。在次优ATP浓度下,D-乳酸刺激蛋白质转运,这表明质子动力势虽然不足以支持转运,但可以促进这一过程。