Li S, Pelka H, Schulman L H
Department of Developmental Biology and Cancer, Albert Einstein College of Medicine, Bronx, New York 10461.
J Biol Chem. 1993 Aug 25;268(24):18335-9.
A gel shift assay that distinguishes the aminoacylated form from the deacylated form of tRNAs was used to study the requirements for aminoacylation of Escherichia coli tRNA(Asn) in vivo. tRNA(Asn) derivatives containing single base changes in their anticodons or discriminator bases were constructed, and the extent of in vivo aminoacylation was determined directly. Substitution of U35 with C35 or U36 with C36 abolished aminoacylation of the tRNA. Substitution of G34 with C34 converted tRNA(Asn) into a lysine acceptor. Thus, each of the anticodon nucleotides are important for aminoacylation of tRNA(Asn). Substitution of discriminator base G73 with A73 affected the extent of aminoacylation in vivo indicating that the discriminator base also contributes to aminoacylation of tRNA(Asn).
一种能区分tRNA氨酰化形式和去氨酰化形式的凝胶迁移分析方法被用于研究大肠杆菌tRNA(Asn)在体内进行氨酰化的条件。构建了反密码子或鉴别碱基中含有单个碱基变化的tRNA(Asn)衍生物,并直接测定了体内氨酰化的程度。将U35替换为C35或U36替换为C36会消除tRNA的氨酰化。将G34替换为C34会使tRNA(Asn)转变为赖氨酸受体。因此,反密码子的每个核苷酸对于tRNA(Asn)的氨酰化都很重要。将鉴别碱基G73替换为A73影响了体内氨酰化的程度,表明鉴别碱基也有助于tRNA(Asn)的氨酰化。