Nazarenko I A, Peterson E T, Zakharova O D, Lavrik O I, Uhlenbeck O C
Novosibirsk State University, Russia.
Nucleic Acids Res. 1992 Feb 11;20(3):475-8. doi: 10.1093/nar/20.3.475.
The specificity of the interaction between tRNAPhe and phenylalanyl-tRNA synthetase isolated from human placenta was investigated. Using yeast tRNAPhe transcripts with different point mutations it was shown that all the five recognition points for the yeast phenylalanyl-tRNA synthetase (G20, G34, A35, A36 and A73) are also important for the reaction catalyzed by the human enzyme. A set of mutations in nucleotides involved in tertiary interactions of tRNAPhe revealed that mutations which maintained the proper folding of the molecule had almost no influence on the efficiency of aminoacylation. The most striking difference between the yeast and human phenylalanyl-tRNA synthetases involved a mutation in the lower two base pairs of the anticodon stem. This mutation did not affect aminoacylation with the yeast enzyme, but greatly reduced activity with human phenylalanyl-tRNA synthetase.
对从人胎盘中分离出的苯丙氨酰 - tRNA合成酶与苯丙氨酸tRNA之间相互作用的特异性进行了研究。使用具有不同点突变的酵母苯丙氨酸tRNA转录本表明,酵母苯丙氨酰 - tRNA合成酶的所有五个识别位点(G20、G34、A35、A36和A73)对人源酶催化的反应也很重要。一组参与苯丙氨酸tRNA三级相互作用的核苷酸突变表明,保持分子正确折叠的突变对氨酰化效率几乎没有影响。酵母和人源苯丙氨酰 - tRNA合成酶之间最显著的差异涉及反密码子茎下部两个碱基对中的一个突变。该突变不影响酵母酶的氨酰化,但大大降低了人源苯丙氨酰 - tRNA合成酶的活性。