Département de Biologie et de Génomique Structurales, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch 67400, France.
Curr Opin Struct Biol. 2010 Jun;20(3):325-32. doi: 10.1016/j.sbi.2010.03.002. Epub 2010 Apr 12.
Recent collection of high-resolution crystal structures of the 70S ribosome with mRNA and tRNA substrates enhances our knowledge of protein synthesis principles. A novel network of interactions between the ribosome in the elongation state and mRNA downstream from the A codon suggests that mRNA is stabilized and aligned at the entrance to the decoding center. The X-ray studies clarify how natural modifications of tRNA are involved in the stabilization of the codon-anticodon interactions, prevention of frame-shifting and also expansion of the decoding capacity of tRNAs. In addition, the crystal structures provide the view that tRNA in the A and P sites communicate through a protein rich environment and suggest how these tRNAs are controlled through the intersubunit bridge formed by protein L31.
最近,通过收集与 mRNA 和 tRNA 底物结合的高分辨率 70S 核糖体晶体结构,我们对蛋白质合成原理有了更深入的了解。在延伸状态下的核糖体与 A 密码子下游的 mRNA 之间存在一种新的相互作用网络,这表明 mRNA 在进入解码中心之前被稳定和排列。X 射线研究阐明了 tRNA 的天然修饰如何参与稳定密码子-反密码子相互作用、防止移码以及扩展 tRNA 的解码能力。此外,晶体结构还提供了一种观点,即 A 位和 P 位的 tRNA 通过富含蛋白质的环境进行通讯,并说明了这些 tRNA 如何通过由 L31 蛋白形成的亚基间桥进行控制。