Yusupova G Z, Belitsina N V, Spirin A S
FEBS Lett. 1986 Sep 29;206(1):142-6. doi: 10.1016/0014-5793(86)81356-4.
Misacylated phenylalanyl-tRNALys, just as lysyl-tRNALys, but not phenylalanyl-tRNAPhe, have been shown to serve as substrates for ribosomal synthesis of polypeptides (polyphenylalanine and polylysine, respectively) in the absence of a template polynucleotide (poly(A)). The conclusion was made that it is the structure of tRNA that determines the ability of the aminoacyl-tRNALys to participate in peptide elongation on ribosomes without codon-anticodon interactions.
已证明,错酰化的苯丙氨酰 - tRNAlys与赖氨酰 - tRNAlys一样,但苯丙氨酰 - tRNAphe则不然,在没有模板多核苷酸(聚腺苷酸)的情况下,它们可分别作为核糖体合成多肽(分别为聚苯丙氨酸和聚赖氨酸)的底物。得出的结论是,正是tRNA的结构决定了氨酰 - tRNAlys在没有密码子 - 反密码子相互作用的情况下参与核糖体上肽链延伸的能力。