Acceptor stem and anticodon RNA hairpin helix interactions with glutamine tRNA synthetase |
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Authors: | DJ Wright SA Martinis M Jahn D Sll P Schimmel |
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Institution: | D.J. Wright, S.A. Martinis, M. Jahn, D. Söll,P. Schimmel, |
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Abstract: | The class I glutamine (Gln) tRNA synthetase interacts with the anticodon and acceptor stem of glutamine tRNA. RNA hairpin helices were designed to probe acceptor stem and anticodon stem-loop contacts. A seven-base pair RNA microhelix derived from the acceptor stem of tRNAGln was aminoacylated by Gln tRNA synthetase. Variants of the glutamine acceptor stem microhelix implicated the discriminator base as a major identity element for glutaminylation of the RNA helix. A second RNA microhelix representing the anticodon stem-loop competitively inhibited tRNAGln charging. However, the anticodon stem-loop microhelix did not enhance aminoacylation of the acceptor stem microhelix. Thus, transduction of the anticodon identity signal may require covalent continuity of the tRNA chain to trigger efficient aminoacylation. |
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Keywords: | tRNA identity genetic code RNA recognition aminoacyl tRNA synthetases evolution of coding |
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