延伸因子G与核糖体L1柄之间的变构协作指导翻译过程中的tRNA运动
Allosteric collaboration between elongation factor G and the ribosomal L1 stalk directs tRNA movements during translation
摘要：
确定转运RNA（tRNA）在翻译过程中快速准确地通过核糖体A、P和E位点转运的机制仍然是蛋白质合成研究的主要目标。在这里，我们报告的实时动态L1柄，一个结构元件的核糖体大亚基，涉及在翻译过程中指导tRNA运动。在易位前的核糖体复合物中，L1柄存在于开放和闭合构象之间的动态平衡中。延伸因子G（EF-G）的结合通过至少两种不同的动力学机制之一将这种平衡向闭合构象转移，其中P-位点tRNA的身份决定了所采取的动力学途径。在易位后复合物中，L1茎动态依赖于E位点tRNA的存在和身份。总的来说，我们的数据表明，EF-G和L1柄变构合作，直接从P到E站点的tRNA易位，并建议一个模型的E-站点tRNA的释放。
英文摘要：
Determining the mechanism by which transfer RNAs (tRNAs) rapidly and precisely transit through the ribosomal A, P and E sites during translation remains a major goal in the study of protein synthesis. Here, we report the real-time dynamics of the L1 stalk, a structural element of the large ribosomal subunit that is implicated in directing tRNA movements during translation. Within pre-translocation ribosomal complexes, the L1 stalk exists in a dynamic equilibrium between open and closed conformations. Binding of elongation factor G (EF-G) shifts this equilibrium towards the closed conformation through one of at least two distinct kinetic mechanisms, where the identity of the P-site tRNA dictates the kinetic route that is taken. Within post-translocation complexes, L1 stalk dynamics are dependent on the presence and identity of the E-site tRNA. Collectively, our data demonstrate that EF-G and the L1 stalk allosterically collaborate to direct tRNA translocation from the P to the E sites, and suggest a model for the release of E-site tRNA.
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