Bubunenko M G, Kireeva M L, Gudkov A T
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region.
Biochimie. 1992 May;74(5):419-25. doi: 10.1016/0300-9084(92)90081-o.
Interactions of EF-Ts with EF-Tu at all steps of the elongation cycle were studied by limited trypsinolysis, gel-filtration, analytical centrifugation and fluorescence polarization techniques. It is shown that EF-Ts does not dissociate from EF-Tu after GDP to GTP exchange, but remains bound to the Aa-tRNA.EF-Tu.GTP complex up to GTP hydrolysis stage on the ribosome. The possible role of these interactions is discussed.
通过有限胰蛋白酶水解、凝胶过滤、分析超速离心和荧光偏振技术研究了延伸循环各步骤中EF-Ts与EF-Tu的相互作用。结果表明，GDP与GTP交换后，EF-Ts不会从EF-Tu上解离，而是在核糖体上GTP水解阶段之前一直与氨酰-tRNA·EF-Tu·GTP复合物结合。讨论了这些相互作用的可能作用。
