McClain W H
Department of Bacteriology, University of Wisconsin, Madison 53706-1567.
J Biol Chem. 1993 Sep 15;268(26):19398-402.
The in vivo aminoacylation specificity of tRNA(Cys) was studied with mutants of opal and amber suppressor tRNAs in Escherichia coli. This specificity depends not only on nucleotides in the acceptor end and anticodon of tRNA(Cys), but also on nucleotides in the dihydrouridine stem and loop and the variable loop that interact, forming the complex core of tRNA tertiary structure.
利用大肠杆菌中乳白抑制型tRNA和琥珀抑制型tRNA的突变体，对tRNA（Cys）的体内氨酰化特异性进行了研究。这种特异性不仅取决于tRNA（Cys）受体端和反密码子中的核苷酸，还取决于二氢尿嘧啶茎环和可变环中相互作用的核苷酸，这些核苷酸形成了tRNA三级结构的复合核心。
