Kostiashkina O E, Asatrian L S, Gavrilova L P, Spirin A S
Mol Biol (Mosk). 1975 Sep-Oct;9(5):775-82.
A comparison of the effect of 11 antibiotic inhibitors of protein synthesis on "enzymatic" and para-chloromercuribenzoateactivated "non-enzymatic" translation was made. It was found that fusidic acid which inhibits protein synthesis by blocking the action of one of the elongation factors (EF-G) did not suppress functioning of the "non-enzymatic" system. On the contrary, all the antibiotics blocking different functional sites of the ribosome itself such as tetracycline, chloramphenicol, erythromycin, edeine, thiostreptone, viridogrisein, spectinomycin, streptomycin, kanamycin and neomycin, were shown to inhibit the "non-enzymatic" translation. The data obtained corroborate the idea that the molecular mechanism which the ribosome utilized during "non-enzymatic" translation are similar or identical to the mechanism of normal "enzymatic" translation. It was found that the "non-enzymatic" working ribosome is more sensitive to all the antibiotics as compared to the ribosome synthesizing peptide with the participation of elongation factors (EF-T and EF-G). This suggests that the elongation factors increase the level of general resistance of the working ribosome against very different hindrances.
对11种蛋白质合成抗生素抑制剂对“酶促”和对氯汞苯甲酸激活的“非酶促”翻译的影响进行了比较。发现通过阻断延伸因子之一(EF-G)的作用来抑制蛋白质合成的夫西地酸不会抑制“非酶促”系统的功能。相反,所有阻断核糖体本身不同功能位点的抗生素,如四环素、氯霉素、红霉素、伊短菌素、硫链丝菌素、绿灰霉素、壮观霉素、链霉素、卡那霉素和新霉素,均显示出抑制“非酶促”翻译的作用。所获得的数据证实了这样一种观点,即核糖体在“非酶促”翻译过程中所利用的分子机制与正常“酶促”翻译的机制相似或相同。研究发现,与在延伸因子(EF-T和EF-G)参与下合成肽的核糖体相比,“非酶促”工作核糖体对所有抗生素更为敏感。这表明延伸因子提高了工作核糖体对非常不同阻碍的总体抗性水平。