REVIEW: Interaction of Aminoacyl-tRNA Synthetases with tRNA: General Principles and Distinguishing Characteristics of the High-Molecular-Weight Substrate Recognition

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I. A. Vasil'eva and N. A. Moor^*

Institute of Chemical Biology and Fundamental Medicine, Siberian Division of the Russian Academy of Sciences, pr. Lavrentieva 8, 630090 Novosibirsk, Russia; fax: (383) 333-3677; E-mail: moor@niboch.nsc.ru

^* To whom correspondence should be addressed.

Received September 29, 2006; Revision received November 29, 2006

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This review summarizes results of numerous (mainly functional) studies that have been accumulated over recent years on the problem of tRNA recognition by aminoacyl-tRNA synthetases. Development and employment of approaches that use synthetic mutant and chimeric tRNAs have demonstrated general principles underlying highly specific interaction in different systems. The specificity of interaction is determined by a certain number of nucleotides and structural elements of tRNA (constituting the set of recognition elements or specificity determinants), which are characteristic of each pair. Crystallographic structures available for many systems provide the details of the molecular basis of selective interaction. Diversity and identity of biochemical functions of the recognition elements make substantial contribution to the specificity of such interactions.

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KEY WORDS: aminoacyl-tRNA synthetase, protein-RNA interaction, specificity, tRNA recognition

DOI: 10.1134/S0006297907030029

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