McClain W H, Foss K
Department of Bacteriology, University of Wisconsin, Madison 53706.
Science. 1988 Sep 30;241(4874):1804-7. doi: 10.1126/science.2459773.
The specificity of tRNA(Arg) (arginine transfer RNA) for aminoacylation (its acceptor identity) were first identified by computer analysis and then examined with amber suppressor tRNAs in Escherichia coli. On replacing two nucleotides in tRNA(Phe) (phenylalanine transfer RNA) with the corresponding nucleotides from tRNA(Arg), the acceptor identity of the resulting tRNA was changed to that of tRNA(Arg). The nucleotides used in the identity transformation occupy a "variable pocket" structure on the surface of the tRNA molecule where two single-stranded loop segments interact. The middle nucleotide in the anticodon also probably contributes to the interaction, since an amber suppressor of tRNA(Arg) had an acceptor identity for lysine as well as arginine.
tRNA（精氨酸转运RNA）用于氨酰化的特异性（其受体识别特性）首先通过计算机分析得以确定，随后在大肠杆菌中利用琥珀抑制tRNA进行了检验。用tRNA（精氨酸）中的相应核苷酸替换tRNA（苯丙氨酸）中的两个核苷酸后，所得tRNA的受体识别特性转变为tRNA（精氨酸）的特性。在身份转变中所使用的核苷酸占据了tRNA分子表面的一个“可变口袋”结构，在该结构中两个单链环段相互作用。反密码子中的中间核苷酸可能也对这种相互作用有贡献，因为tRNA（精氨酸）的一个琥珀抑制子对赖氨酸以及精氨酸都具有受体识别特性。
