Recognition nucleotides for human phenylalanyl-tRNA synthetase.
Recognition nucleotides for human phenylalanyl-tRNA synthetase.
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人苯丙氨酰-tRNA 合成酶的识别核苷酸。
DOI：
10.1093/nar/20.3.475
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发表时间：
1992
影响因子：
14.9
通讯作者：
Uhlenbeck,OC
中科院分区：
文献类型：
--
作者：
Nazarenko,IA;Peterson,ET;Zakharova,OD;Lavrik,OI;Uhlenbeck,OC
本文研究了人胎盘组织中分离的苯丙氨酰-tRNA合成酶与tRNAp相互作用的特异性。利用具有不同点突变的酵母tRNAPhetrase，发现酵母苯氧基-tRGSSA合成酶的5个识别点(G20、G34、A35、A36和A73)对人酶催化的反应也是重要的。在tRNAP的三级相互作用中涉及的一组核苷酸突变)表明，维持分子正确折叠的突变几乎不影响氨基酰化反应的效率。酵母和人类苯丙氨酰-tRNA合成酶之间最显著的区别是反密码子茎的低两个碱基对发生了突变。该突变不影响与酵母酶的氨酰化，但极大地降低了与人苯丙氨酰-tRNA合成酶的活性。
The specificity of the interaction between tRNAPheand phenyBalanyl-tRNA synthetase isolated from human placenta was investigated. Using yeast tRNAPhetranscripts with different point mutations it was shown that all the five recognition points for the yeast phenylaOanyl-tRGSSA synthetase (G20, G34, A35, A36and A73) are also important for the reaction catalyzed by the human enzyme. A set of mutations in nucleotides involved) in tertiary interactions of tRNAPherevealed that mutations which maintained the proper folding of the molecuOe had almost no influence on the efficiency of amieioacylation. 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.