Translation of non-standard codon nucleotides reveals minimal requirements for codon-anticodon interactions

Thomas Philipp Hoernes, Klaus Faserl, Michael Andreas Juen, Johannes Kremser, Catherina Gasser, Elisabeth Fuchs, Xinying Shi, Aaron Siewert, Herbert Lindner, Christoph Kreutz, Ronald Micura, Simpson Joseph, Claudia Höbartner, Eric Westhof, Alexander Hüttenhofer and Matthias David Erlacher ()
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Thomas Philipp Hoernes: Medical University of Innsbruck
Klaus Faserl: Medical University of Innsbruck
Michael Andreas Juen: University of Innsbruck
Johannes Kremser: University of Innsbruck
Catherina Gasser: University of Innsbruck
Elisabeth Fuchs: University of Innsbruck
Xinying Shi: University of California at San Diego
Aaron Siewert: University of Würzburg, Am Hubland
Herbert Lindner: Medical University of Innsbruck
Christoph Kreutz: University of Innsbruck
Ronald Micura: University of Innsbruck
Simpson Joseph: University of California at San Diego
Claudia Höbartner: University of Würzburg, Am Hubland
Eric Westhof: Institute of Molecular and Cellular Biology of the CNRS UPR9002/University of Strasbourg
Alexander Hüttenhofer: Medical University of Innsbruck
Matthias David Erlacher: Medical University of Innsbruck

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: Abstract The precise interplay between the mRNA codon and the tRNA anticodon is crucial for ensuring efficient and accurate translation by the ribosome. The insertion of RNA nucleobase derivatives in the mRNA allowed us to modulate the stability of the codon-anticodon interaction in the decoding site of bacterial and eukaryotic ribosomes, allowing an in-depth analysis of codon recognition. We found the hydrogen bond between the N1 of purines and the N3 of pyrimidines to be sufficient for decoding of the first two codon nucleotides, whereas adequate stacking between the RNA bases is critical at the wobble position. Inosine, found in eukaryotic mRNAs, is an important example of destabilization of the codon-anticodon interaction. Whereas single inosines are efficiently translated, multiple inosines, e.g., in the serotonin receptor 5-HT2C mRNA, inhibit translation. Thus, our results indicate that despite the robustness of the decoding process, its tolerance toward the weakening of codon-anticodon interactions is limited.

Date: 2018
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DOI: 10.1038/s41467-018-07321-8

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