TY  - JOUR
A1  - Hoernes, Thomas Philipp
A1  - Faserl, Klaus
A1  - Juen, Michael Andreas
A1  - Kremser, Johannes
A1  - Gasser, Catherina
A1  - Fuchs, Elisabeth
A1  - Shi, Xinying
A1  - Siewert, Aaron
A1  - Lindner, Herbert
A1  - Kreutz, Christoph
A1  - Micura, Ronald
A1  - Joseph, Simpson
A1  - Höbartner, Claudia
A1  - Westhof, Eric
A1  - Hüttenhofer, Alexander
A1  - Erlacher, Matthias David
T1  - Translation of non-standard codon nucleotides reveals minimal requirements for codon-anticodon interactions
JF  - Nature Communications
N2  - 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.
KW  - chemical modification
KW  - nucleic acids
KW  - ribozymes
KW  - RNA
Y1  - 2018
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-321067
VL  - 9
ER  -