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Nucleic Acids Research Advance Access originally published online on September 1, 2007
Nucleic Acids Research 2007 35(18):6094-6102; doi:10.1093/nar/gkm534
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Nucleic Acids Research, 2007, Vol. 35, No. 18 6094-6102
© 2007 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.

Nucleic Acid Enzymes

An aminoacyl-tRNA synthetase:elongation factor complex for substrate channeling in archaeal translation

Corinne D. Hausmann1, Mette Prætorius-Ibba1,2 and Michael Ibba1,3,*

1Department of Microbiology, 2Department of Molecular Genetics, 3Ohio State Biochemistry Program, and Ohio State RNA Group, The Ohio State University, Columbus, Ohio 43210-1292, USA

*To whom correspondence should be addressed. Tel: +1 614 292 2120; Fax: +1 614 292 8120; Email: ibba.1{at}osu.edu

Received June 6, 2007. Revised June 25, 2007. Accepted June 30, 2007.

Translation requires the specific attachment of amino acids to tRNAs by aminoacyl-tRNA synthetases (aaRSs) and the subsequent delivery of aminoacyl-tRNAs to the ribosome by elongation factor 1 alpha (EF-1{alpha}). Interactions between EF-1{alpha} and various aaRSs have been described in eukaryotes, but the role of these complexes remains unclear. To investigate possible interactions between EF-1{alpha} and other cellular components, a yeast two-hybrid screen was performed for the archaeon Methanothermobacter thermautotrophicus. EF-1{alpha} was found to form a stable complex with leucyl-tRNA synthetase (LeuRS; KD = 0.7 µM). Complex formation had little effect on EF-1{alpha} activity, but increased the kcat for Leu-tRNALeu synthesis ~8-fold. In addition, EF-1{alpha} co-purified with the archaeal multi-synthetase complex (MSC) comprised of LeuRS, LysRS and ProRS, suggesting the existence of a larger aaRS:EF-1{alpha} complex in archaea. These interactions between EF-1{alpha} and the archaeal MSC contribute to translational fidelity both by enhancing the aminoacylation efficiencies of the three aaRSs in the complex and by coupling two stages of translation: aminoacylation of cognate tRNAs and their subsequent channeling to the ribosome.


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