Interactions of Transfer RNAs with their Biological Partners

Ebel, J. P.; Giege, R.; Moras, D.; Remy, P.

doi:10.1007/978-94-009-6457-0_10

J. P. Ebel²,
R. Giege²,
D. Moras² &
…
P. Remy²

36 Accesses

Abstract

The three-dimensional structure of two elongator tRNAs, tRNA^Phe and tRNA^Asp from yeast, has been solved at high resolution. Their secondary cloverleaf structures are folded in a tertiary L-shaped conformation with a more open structure for tRNA^Asp. Both tRNAs present different molecular dynamics as revealed by temperature factors of the different parts of the molecules. These features are related to different conformational states of the tRNAs: tRNA^Phe would possess the structure of a free tRNA and tRNA^Asp that of a tRNA on the ribosome. The solution structure of both tRNAs was probed with chemical reagents and compared with the crystal structures. Structural similarities as well as differences were detected reflecting the versatility of tRNA structures.

Comparing the accessibility of tRNAs, in their free state and complexed to aminoacyl-tRNA synthetases or elongation factor EF-Tu, to chemical or enzymatic probes, it was possible to determine the regions of tRNAs in close contact with their macromolecular partners. Upon complex formation with aminoacyl- tRNA synthetases a multistep adaptation of both macromolecules takes place, analogous to an induced fit. This process determines the specificity of the tRNA aminoacylation reaction. In the particular case of the yeast phenylalanine system, the wybutine residue next to the anticodon of tRNA^Phe has been identified as an important element in this mechanism. More precise structural information will arise in future from studies on crystallized complexes. Such a complex, that between tRNA^Asp and aspartyl-tRNA synthetase, has been crystallized and is under investigation.

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Institut de Biologie Moléculaire et Cellulaire du CNRS, 15, rue René Descartes, 67084, Strasbourg, France
J. P. Ebel, R. Giege, D. Moras & P. Remy

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J. P. Ebel
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R. Giege
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D. Moras
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Institut de Biologie Physico-Chimique, Fondation Edmond de Rothschild, 13 rue Pierre et Marie Curie, 75005, Paris, France
B. Pullman

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Ebel, J.P., Giege, R., Moras, D., Remy, P. (1984). Interactions of Transfer RNAs with their Biological Partners. In: Chagas, C., Pullman, B. (eds) Specificity in Biological Interactions. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-6457-0_10

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