Cundliffe E, Thompson J
Eur J Biochem. 1981 Aug;118(1):47-52. doi: 10.1111/j.1432-1033.1981.tb05484.x.
The antibiotic, micrococcin, binds to complexes formed between bacterial 23-S ribosomal RNA and ribosomal protein L11 and, in doing so, inhibits of thiostrepton. In assay systems simulating partial reaction of protein synthesis, micrococcin inhibits a number of processes believed to involve the ribosomal A site while stimulating GTP hydrolysis dependent upon ribosomes and elongation factor EF-G. The latter effect is not observed upon ribosomes lacking a protein homologous with protein L11. Nor is it apparent upon those containing 23-S RNA previously subjected to the action of a specific methylase known to render ribosomes resistant to thiostrepton. It is concluded that stimulation by micrococcin of factor-dependent GTP hydrolysis results from the binding of the drug to its normal target site which involves 23-S RNA and protein L11.
抗生素微球菌素与细菌23 - S核糖体RNA和核糖体蛋白L11形成的复合物结合，在此过程中，它抑制硫链丝菌素。在模拟蛋白质合成部分反应的测定系统中，微球菌素抑制了一些被认为涉及核糖体A位点的过程，同时刺激了依赖核糖体和延伸因子EF - G的GTP水解。在缺乏与蛋白L11同源蛋白的核糖体上未观察到后一种效应。在含有先前经已知能使核糖体对硫链丝菌素产生抗性的特定甲基化酶作用的23 - S RNA的核糖体上也不明显。得出的结论是，微球菌素对因子依赖性GTP水解的刺激是由于药物与其正常靶位点结合所致，该靶位点涉及23 - S RNA和蛋白L11。
