Kinjo M, Ishigami M, Hasegawa T, Nagano K
J Mol Evol. 1984;20(1):59-65. doi: 10.1007/BF02101986.
Interaction based on possible chemical affinity of an amino acid for tRNA was examined as a model for the aminoacylation of primitive tRNA without aid of an enzyme system. Two types of reaction were carried out and compared. One was the acyl linkage of amino acid to the 5'-terminal phosphate of a tRNA activated as an imidazolide. The other was the incorporation of an amino acid activated as an imidazolide into 2'(3')-hydroxyl groups of intact tRNA. Both types of reaction indicated that none of the amino acids tested had any selectivity for the tRNAs examined. However, the rates of reaction with a given tRNA were different among amino acids. In the second type of reaction, amino acids were found mainly at loop-out regions of tRNA, but not at either its 5'- or 3'-terminal sites.
基于氨基酸与tRNA可能的化学亲和力的相互作用被作为无酶系统辅助的原始tRNA氨酰化模型进行了研究。进行并比较了两种类型的反应。一种是氨基酸与作为咪唑化物活化的tRNA的5'-末端磷酸形成酰基连接。另一种是作为咪唑化物活化的氨基酸掺入完整tRNA的2'(3')-羟基中。两种类型的反应均表明，所测试的氨基酸对所研究的tRNA均无任何选择性。然而，不同氨基酸与给定tRNA的反应速率不同。在第二种类型的反应中，发现氨基酸主要位于tRNA的环出区域，而不在其5'-或3'-末端位点。
