Kolb A J, Redfield B, Twardowski T, Weissbach H
Biochim Biophys Acta. 1978 Jul 24;519(2):398-405. doi: 10.1016/0005-2787(78)90093-x.
The present study has examined the requirements for the binding of rabbit reticulocyte elongation factor 1 (EF-1) to ribosomes under different assay conditions. When a centrifugation procedure was used to separate the ribosome EF-1 complex, the binding of EF-1 to ribosomes required GTP and Phe-tRNA, but not poly(U). The results suggested that undr these conditions a ternary complex, EF-1 . GTP . aminoacyl-tRNA, is necessary for the formation of a ribosome . EF-1 complex. However, when gel filtration was used to isolate the ribosome . EF-1 complex, only template and tRNA were required. These studie emphasize the fact that the procedure used to isolate the ribosome . EF-1 complex determines the requirements for stable complex formation. EF-1 can also interact with nucleic acids such as 28 S and 18 S rRNA, messenger RNA and DNA. In contrast to the binding to ribosomes, EF-1 binding to nucleic acids requires only Mg2+.
本研究检测了在不同测定条件下兔网织红细胞延伸因子1（EF-1）与核糖体结合的条件。当采用离心程序分离核糖体-EF-1复合物时，EF-1与核糖体的结合需要GTP和苯丙氨酰-tRNA，但不需要聚尿苷酸（poly(U)）。结果表明，在这些条件下，三元复合物EF-1·GTP·氨酰-tRNA对于核糖体-EF-1复合物的形成是必需的。然而，当使用凝胶过滤法分离核糖体-EF-1复合物时，仅需要模板和tRNA。这些研究强调了用于分离核糖体-EF-1复合物的程序决定了稳定复合物形成条件这一事实。EF-1还能与诸如28 S和18 S核糖体RNA、信使RNA和DNA等核酸相互作用。与和核糖体的结合不同，EF-1与核酸的结合仅需要Mg2+。
