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Nucleic Acids Research Advance Access originally published online on March 26, 2008
Nucleic Acids Research 2008 36(8):2728-2738; doi:10.1093/nar/gkn028
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Nucleic Acids Research, 2008, Vol. 36, No. 8 2728-2738
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

RNA

Recognition of tRNALeu by Aquifex aeolicus leucyl-tRNA synthetase during the aminoacylation and editing steps

Peng Yao1, Bin Zhu1, Sophie Jaeger1,2, Gilbert Eriani1,2 and En-Duo Wang1,*

1State Key Laboratory of Molecular Biology – Graduate School of the Chinese Academy of Sciences, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, Shanghai 200031, People's Republic of China and 2UPR9002 du CNRS, Architecture et Réactivité de l’ARN, Université Louis Pasteur, 67084 Strasbourg, France

*To whom correspondence should be addressed. Tel: +86 21 54921241; Fax: +86 21 54921011; Email: edwang{at}sibs.ac.cn

Received August 19, 2007. Revised January 17, 2008. Accepted January 17, 2008.

Recognition of tRNA by the cognate aminoacyl-tRNA synthetase during translation is crucial to ensure the correct expression of the genetic code. To understand tRNALeu recognition sets and their evolution, the recognition of tRNALeu by the leucyl-tRNA synthetase (LeuRS) from the primitive hyperthermophilic bacterium Aquifex aeolicus was studied by RNA probing and mutagenesis. The results show that the base A73; the core structure of tRNA formed by the tertiary interactions U8–A14, G18–U55 and G19–C56; and the orientation of the variable arm are critical elements for tRNALeu aminoacylation. Although dispensable for aminoacylation, the anticodon arm carries discrete editing determinants that are required for stabilizing the conformation of the post-transfer editing state and for promoting translocation of the tRNA acceptor arm from the synthetic to the editing site.


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