Ogawa K, Nishikawa K, Takemura S
Department of Molecular Biology, School of Science, Nagoya University, Japan.
Nucleic Acids Symp Ser. 1988(19):125-8.
By enzymatic cleavage and ligation of tRNAVa1, its anticodon sequence IAC was altered to IAU, the anticodon of tRNAI1e. Valine acceptor activity of this variant tRNAVa1 (IAU) was reduced to the extent much lower than tyrosine acceptability of the previously prepared tRNATyr (GAA) (anticodon for tRNAPhe). Isoleucine acceptor activity was undetected, contrary to tRNATyr (GAA) which accepted phenylalanine weakly. Cleavage of tRNAVa1 (IAC) between IACA37 and C38 of its anticodon loop reduced the valine acceptor activity, suggesting some contribution of the conformation of the anticodon loop to the aminoacylation reaction.
通过对tRNAVal进行酶切和连接，其反密码子序列IAC被改变为tRNAIle的反密码子IAU。这种变体tRNAVal（IAU）的缬氨酸接受活性降低到远低于先前制备的tRNATyr（GAA）（tRNAPhe的反密码子）的酪氨酸接受性的程度。未检测到异亮氨酸接受活性，这与弱接受苯丙氨酸的tRNATyr（GAA）相反。在其反密码子环的IACA37和C38之间切割tRNAVal（IAC）降低了缬氨酸接受活性，表明反密码子环的构象对氨酰化反应有一定贡献。
