Dale Taraka, Uhlenbeck Olke C
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA.
Trends Biochem Sci. 2005 Dec;30(12):659-65. doi: 10.1016/j.tibs.2005.10.006. Epub 2005 Nov 2.
Recent structural and biochemical experiments indicate that bacterial elongation factor Tu and the ribosomal A-site show specificity for both the amino acid and the tRNA portions of their aminoacyl-tRNA (aa-tRNA) substrates. These data are inconsistent with the traditional view that tRNAs are generic adaptors in translation. We hypothesize that each tRNA sequence has co-evolved with its cognate amino acid, such that all aa-tRNAs are translated uniformly.
最近的结构和生化实验表明，细菌延伸因子Tu和核糖体A位点对其氨酰-tRNA（aa-tRNA）底物的氨基酸和tRNA部分均表现出特异性。这些数据与tRNA在翻译中是通用适配器的传统观点不一致。我们假设每个tRNA序列与其同源氨基酸共同进化，从而使所有aa-tRNA都能被统一翻译。
