Document Type
Article
Publication Date
9-1-2007
Abstract
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-1α). Interactions between EF-1α and various aaRSs have been described in eukaryotes, but the role of these complexes remains unclear. To investigate possible interactions between EF-1α and other cellular components, a yeast two-hybrid screen was performed for the archaeon Methanothermobacter thermautotrophicus. EF-1α was found to form a stable complex with leucyl-tRNA synthetase (LeuRS; KD = 0.7 μ M). Complex formation had little effect on EF-1α activity, but increased the kcat for Leu-tRNALeu synthesis ∼ 8-fold. In addition, EF-1α co-purified with the archaeal multi-synthetase complex (MSC) comprised of LeuRS, LysRS and ProRS, suggesting the existence of a larger aaRS:EF-1α complex in archaea. These interactions between EF-1α 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.
Recommended Citation
Hausmann, C.D., Prætorius-Ibba, M. and Ibba, M. (2007) An aminoacyl-tRNA synthetase: elongation factor complex for substrate channeling in archaeal translation. Nucleic Acids Res. 35, 6094-6102. https://doi.org/10.1093/nar/gkm534
Copyright
The authors
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial 2.0 License
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Amino Acids, Peptides, and Proteins Commons, Biochemistry Commons, Cellular and Molecular Physiology Commons, Molecular Biology Commons, Nucleic Acids, Nucleotides, and Nucleosides Commons, Other Biochemistry, Biophysics, and Structural Biology Commons
Comments
This article was originally published in Nucleic Acids Research, volume 35, in 2007. https://doi.org/10.1093/nar/gkm534