Tanada S, Kawakami M, Nishio K, Takemura S
J Biochem. 1982 Jan;91(1):291-9. doi: 10.1093/oxfordjournals.jbchem.a133687.
The present investigation was undertaken to see to what extent the alpha-amino group of the amino acid, the side chain of the amino acid of aminoacyl-tRNA, and the tRNA structure are involved in determining the affinity of aminoacyl-tRNA for bacterial elongation factor Tu-GTP complex. Various aminoacyl-tRNAs, mis-aminoacylated tRNAs, and formylated aminoacyl-tRNAs were prepared, and the dissociation constants of the ternary complexes of aminoacyl-tRNA with ET-Tu: GTP were determined by the RNase-resistance assay. The results indicated that the free amino-acid group of the amino acids in aminoacyl-tRNA is strongly required for binding with EF-Tu : GTP. In this concentration, the biological significance of formylation for Met-tRNAMetf species is discussed.
本研究旨在探讨氨基酸的α-氨基、氨酰-tRNA中氨基酸的侧链以及tRNA结构在多大程度上参与决定氨酰-tRNA对细菌延伸因子Tu-GTP复合物的亲和力。制备了各种氨酰-tRNA、错配氨酰化tRNA和甲酰化氨酰-tRNA，并通过核糖核酸酶抗性测定法测定了氨酰-tRNA与ET-Tu:GTP三元复合物的解离常数。结果表明，氨酰-tRNA中氨基酸的游离氨基基团对于与EF-Tu:GTP结合是强烈必需的。在此浓度下，讨论了甲酰化对Met-tRNAMetf种类的生物学意义。
