大肠杆菌谷氨酰胺-tRNA合成酶与非同源tRNA的相互作用。

Interaction of Escherichia coli glutaminyl-tRNA synthesis with noncognate tRNA's.

作者信息

Seno T, Nakamura A, Fukuhara S, Iwata K

出版信息

Nucleic Acids Res. 1978 May;5(5):1561-70. doi: 10.1093/nar/5.5.1561.

DOI:10.1093/nar/5.5.1561

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC342104/

Abstract

Several noncognate tRNA's from Escherichia coli were mischarged with glutamine by E. coli glutaminyl-tRNA synthetase if dimethylsulfoxide was present in the reaction mixture. Kinetic analysis of the mischarging revealed that dimethyl sulfoxide stimulated the misacylation by affecting the maximum velocity. Several noncognate tRNA's were shown to interact with glutaminyl-tRNA synthetase as measured by their ability to protect the enzyme against thermal inactivation or to replace cognate tRNA in stimulating glutamine-dependent ATP-PPi exchange reaction. These tRNA's, however, did not coincide with those which were mischargeable with glutamine.

摘要

如果反应混合物中存在二甲基亚砜，来自大肠杆菌的几种非同源tRNA会被大肠杆菌谷氨酰胺-tRNA合成酶错误地负载谷氨酰胺。对这种错误负载的动力学分析表明，二甲基亚砜通过影响最大反应速度来刺激错误酰化。通过它们保护该酶免受热失活的能力或在刺激谷氨酰胺依赖性ATP-PPi交换反应中取代同源tRNA的能力来测量，结果显示几种非同源tRNA与谷氨酰胺-tRNA合成酶相互作用。然而，这些tRNA与那些可被错误负载谷氨酰胺的tRNA并不一致。

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A single mutational modification of a tryptophan-specific transfer RNA permits aminoacylation by glutamine and translation of the codon UAG.对一种色氨酸特异性转运RNA进行单一突变修饰可使其被谷氨酰胺氨酰化，并翻译密码子UAG。

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Involvement of the anticodon region of Escherichia coli tRNAGln and tRNAGlu in the specific interaction with cognate aminoacyl-tRNA synthetase. Alteration of the 2-thiouridine derivatives located in the anticodon of the tRNAs by BrCN or sulfur deprivation.大肠杆菌谷氨酰胺转运RNA（tRNAGln）和谷氨酸转运RNA（tRNAGlu）反密码子区域在与同源氨酰-tRNA合成酶特异性相互作用中的作用。通过溴化氰（BrCN）或硫缺乏改变位于tRNA反密码子中的2-硫代尿苷衍生物。

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Aminoacyl-tRNA synthetases: sone recent results and achievements.氨酰-tRNA合成酶：一些近期的结果与成就

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Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. I. Purification and properties.大肠杆菌谷氨酰胺转移核糖核酸合成酶。I. 纯化及性质

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