Wolf H, Assmann D, Fischer E
Proc Natl Acad Sci U S A. 1978 Nov;75(11):5324-8. doi: 10.1073/pnas.75.11.5324.
Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Hydrolysis of GTP by EF-Tu, induced by aminoacyl-tRNA, ribosomes, and mRNA or by kirromycin, is inhibited by pulvomycin. As shown by Millipore filtration, chromatographic analysis, and hydrolysis protection experiments, pulvomycin prevents interaction between aminoacyl-tRNA and EF-Tu.GTP to yield the ternary complex aminoacyl-tRNA.EF-Tu.GTP. Thus, enzymatic binding of aminoacyl-tRNA to ribosomes is blocked.
已证明普尔沃霉素以及同义抗生素拉比洛霉素和1063-Z通过作用于延伸因子Tu（EF-Tu）来抑制原核生物蛋白质合成：在抗生素存在的情况下，EF-Tu对鸟嘌呤核苷酸的亲和力发生改变，催化EF-Tu.GDP/GTP交换，并刺激EF-Tu.GTP复合物的形成。由氨酰基-tRNA、核糖体和mRNA或由奇霉素诱导的EF-Tu对GTP的水解受到普尔沃霉素的抑制。如通过密理博过滤、色谱分析和水解保护实验所示，普尔沃霉素可防止氨酰基-tRNA与EF-Tu.GTP之间相互作用以产生三元复合物氨酰基-tRNA.EF-Tu.GTP。因此，氨酰基-tRNA与核糖体的酶促结合被阻断。
