Weijland A, Parmeggiani A
S.D.I. 61840 du CNRS, Laboratoire de Biochimie, Ecole Polytechnique, Palaiseau, France.
Trends Biochem Sci. 1994 May;19(5):188-93. doi: 10.1016/0968-0004(94)90018-3.
In the elongation cycle of bacterial protein biosynthesis, the binding of aminoacyl-tRNA (aa-tRNA) to the A-site of mRNA-programmed ribosomes is mediated by elongation factor Tu (EF-Tu) and associated with the hydrolysis of GTP. Recently, in the case of cognate aa-tRNA, the participation of two GTP molecules has been implicated in this reaction. These are likely to be involved in preventing the indiscriminate binding of aa-tRNA to the ribosomal A-site. This article integrates this unexpected finding with our current knowledge of the structure-function relationships of the macro-molecules involved in the elongation cycle.
在细菌蛋白质生物合成的延伸循环中，氨酰tRNA（aa-tRNA）与mRNA编程核糖体的A位点的结合由延伸因子Tu（EF-Tu）介导，并与GTP的水解相关。最近，就同源aa-tRNA而言，该反应涉及两个GTP分子的参与。这些可能参与防止aa-tRNA与核糖体A位点的随意结合。本文将这一意外发现与我们目前对延伸循环中涉及的大分子结构-功能关系的认识相结合。
