RECOGNITION OF TRANSFER-RNAS BY AMINOACYL-TRANSFER RNA-SYNTHETASES
RECOGNITION OF TRANSFER-RNAS BY AMINOACYL-TRANSFER RNA-SYNTHETASES
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DOI：
10.1096/fasebj.7.1.8422978
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发表时间：
1993-01-01
期刊：
影响因子：
4.8
通讯作者：
MORAS, D
中科院分区：
文献类型：
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作者：
CAVARELLI, J;MORAS, D
我们目前对tRNAs被其同源氨酰-tRNA合成酶（阿尔斯）识别的分子机制的理解基本上基于三个信息来源：1）使用体内和体外方法表征tRNA身份决定簇，2）从一级序列分析中对合成酶进行分类：阿尔斯可以根据其ATP结合结构域的空间结构分为两类，3）晶体学研究和溶液研究的结构结果。三阿尔斯和两个复合物的晶体结构，每类一个，已知原子分辨率。tRNA识别有两个结构组成部分。受体末端和活性位点结构域之间的相互作用是类特异性的，并且在GlnRS-tRNA（Gln）和AspRS-tRNA（Asp）复合物的晶体结构中观察到的茎的结合模式可以概括为它们各自的类。位于tRNA分子其他部分的身份决定簇由酶的不同结构域解码。这些蛋白质模块表现出很大的结构多样性。识别过程是系统或子组特定的。
Our present understanding of the molecular mechanisms responsible for the recognition of tRNAs by their cognate aminoacyl-tRNA synthetases (aaRS) is essentially based on three sources of information: 1) the characterization of tRNA identity determinants using in vivo and in vitro approaches, 2) the classification of synthetases from primary sequence analysis: aaRS can be partitioned into two classes according to the spatial structure of their ATP binding domain, and 3) the structural results of crystallographic investigations and solution studies. The crystal structures of three aaRS and two complexes, one of each class, are known to atomic resolution. tRNA recognition has two structural components. The interaction between the acceptor end and the active site domain is class-specific and the binding mode of the stem observed in the crystal structures of GlnRS-tRNA(Gln) and AspRS-tRNA(Asp) complexes can be generalized to their respective classes. Identity determinants located in other parts of the tRNA molecule are decoded by different domains of the enzyme. These protein modules exhibit a large structural diversity. The recognition process is then system or subgroup specific.