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Science 21 February 1992:
Vol. 255. no. 5047, pp. 994 - 996
DOI: 10.1126/science.1372129
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Articles

Science, Vol 255, Issue 5047, 994-996
Copyright © 1992 by American Association for the Advancement of Science

articles

The specificity of translational control switched with transfer RNA identity rules

M Graffe, J Dondon, J Caillet, P Romby, C Ehresmann, B Ehresmann, and M Springer

Institut de Biologie Physico-Chimique, Paris, France.

The interaction of Escherichia coli threonyl-transfer RNA (tRNA) synthetase with the leader sequence of its own messenger RNA inhibits ribosome binding, resulting in negative translational feedback regulation. The leader sequence resembles the substrate (tRNA(Thr)) of the enzyme, and the nucleotides that mediate the correct recognition of the leader and the tRNA may be the same. A mutation suggested by tRNA identity rules that switches the resemblance of the leader sequence from tRNA(Thr) to tRNA(Met) causes the translation of the threonyl-tRNA synthetase messenger RNA to become regulated by methionyl-tRNA synthetase. This identity swap in the leader messenger RNA indicates that tRNA identity rules may be extended to interactions of synthetases with other RNAs.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Translational Operator of mRNA on the Ribosome: How Repressor Proteins Exclude Ribosome Binding.
L. Jenner, P. Romby, B. Rees, C. Schulze-Briese, M. Springer, C. Ehresmann, B. Ehresmann, D. Moras, G. Yusupova, and M. Yusupov (2005)
Science 308, 120-123
   Abstract »    Full Text »    PDF »
Resected RNA pseudoknots and their recognition by histidyl-tRNA synthetase.
B. Felden and R. Giege (1998)
PNAS 95, 10431-10436
   Abstract »    Full Text »    PDF »


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