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Nucleic Acids Research 2004 32(17):5076-5086; doi:10.1093/nar/gkh843
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Published online 27 September 2004

Nucleic Acids Research, Vol. 32 No. 17 © Oxford University Press 2004; all rights reserved

A yeast arginine specific tRNA is a remnant aspartate acceptor

Aurélie Fender, Renaud Geslain, Gilbert Eriani, Richard Giegé, Marie Sissler and Catherine Florentz*

Département ‘Mécanismes et Macromolécules de la Synthèse Protéique et Cristallogenèse’, UPR 9002, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15, rue René Descartes, F-67084 Strasbourg Cedex, France

* To whom correspondence should be addressed. Tel: +33 3 88 41 70 59; Fax: +33 3 88 60 22 18; Email: c.florentz{at}ibmc.u-strasbg.fr
Present address: Renaud Geslain, Barcelona Institute of Biomedical Research, Barcelona Science Park, University of Barcelona, Josep Samitier 1–5, Barcelona E-08028, Spain

Received July 1, 2004; Revised and Accepted September 3, 2004

High specificity in aminoacylation of transfer RNAs (tRNAs) with the help of their cognate aminoacyl-tRNA synthetases (aaRSs) is a guarantee for accurate genetic translation. Structural and mechanistic peculiarities between the different tRNA/aaRS couples, suggest that aminoacylation systems are unrelated. However, occurrence of tRNA mischarging by non-cognate aaRSs reflects the relationship between such systems. In Saccharomyces cerevisiae, functional links between arginylation and aspartylation systems have been reported. In particular, it was found that an in vitro transcribed tRNAAsp is a very efficient substrate for ArgRS. In this study, the relationship of arginine and aspartate systems is further explored, based on the discovery of a fourth isoacceptor in the yeast genome, . This tRNA has a sequence strikingly similar to that of tRNAAsp but distinct from those of the other three arginine isoacceptors. After transplantation of the full set of aspartate identity elements into the four arginine isoacceptors, gains the highest aspartylation efficiency. Moreover, it is possible to convert into an aspartate acceptor, as efficient as tRNAAsp, by only two point mutations, C38 and G73, despite the absence of the major anticodon aspartate identity elements. Thus, cryptic aspartate identity elements are embedded within . The latent aspartate acceptor capacity in a contemporary tRNAArg leads to the proposal of an evolutionary link between and tRNAAsp genes.


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