Alpha-sarcin cleavage of ribosomal RNA is inhibited by the binding of elongation factor G or thiostrepton to the ribosome.
Alpha-sarcin cleavage of ribosomal RNA is inhibited by the binding of elongation factor G or thiostrepton to the ribosome.
复制标题
核糖体 RNA 的 α-sarcin 裂解受到延伸因子 G 或硫链丝菌素与核糖体结合的抑制。
DOI：
10.1093/nar/19.7.1657
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发表时间：
1991
影响因子：
14.9
通讯作者：
Bodley,JW
中科院分区：
文献类型：
--
作者：
Miller,SP;Bodley,JW
延伸因子G（EF-G）催化的转位反应可被α-八叠球菌素切割23 SrRNA或硫链丝菌素与E.大肠核糖体在这里，我们表明EF-G和GDP与核糖体的短暂结合抑制了α-八叠球菌素的切割速率，并且与夫西地酸的这种结合的稳定完全阻止了α-八叠球菌素的切割。在延伸因子2与S的结合上观察到类似的抑制模式。空气体抗生素硫链丝菌素与E.另一方面，coliribosome使α-sarcin的分裂速率降低约2倍。这些结果表明，α-sarcin位点位于EF-G结合的核糖体结构域内，并且该位点的构象受硫链丝菌素结合的影响。
The translocatlon reaction catalyzed by elongation factor G (EF-G) is inhibited either by α-sarcin cleavage of 23S rRNA or by the binding of thiostrepton to theE. coliribosome. Here we show that the transitory binding of EF-G and GDP to the ribosome inhibited the rate of α-sarcin cleavage and that stabilization of this binding with fusidic acid completely prevented α-sarcin cleavage. A similar pattern of inhibition was seen upon the binding of elongation factor 2 to theS. cerevisiaeribosome. The irreversible binding of the antibiotic thiostrepton to theE. coliribosome, on the other hand, decreased the rate of cleavage by α-sarcin approximately 2-fold. These results suggest that the α-sarcin site is located within the ribosomal domain for EF-G binding and that the conformation of this site is affected by the binding of thiostrepton.