Novel base-pairing interactions at the tRNA wobble position crucial for accurate reading of the genetic code

Alexey Rozov, Natalia Demeshkina, Iskander Khusainov, Eric Westhof, Marat Yusupov and Gulnara Yusupova ()
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Alexey Rozov: Institute of Genetics and Molecular and Cellular Biology, INSERM, U964; CNRS/University of Strasbourg
Natalia Demeshkina: Institute of Genetics and Molecular and Cellular Biology, INSERM, U964; CNRS/University of Strasbourg
Iskander Khusainov: Institute of Genetics and Molecular and Cellular Biology, INSERM, U964; CNRS/University of Strasbourg
Eric Westhof: Architecture and Reactivity of RNA, Institute of Molecular and Cellular Biology of the CNRS, University of Strasbourg
Marat Yusupov: Institute of Genetics and Molecular and Cellular Biology, INSERM, U964; CNRS/University of Strasbourg
Gulnara Yusupova: Institute of Genetics and Molecular and Cellular Biology, INSERM, U964; CNRS/University of Strasbourg

Nature Communications, 2016, vol. 7, issue 1, 1-10

Abstract: Abstract Posttranscriptional modifications at the wobble position of transfer RNAs play a substantial role in deciphering the degenerate genetic code on the ribosome. The number and variety of modifications suggest different mechanisms of action during messenger RNA decoding, of which only a few were described so far. Here, on the basis of several 70S ribosome complex X-ray structures, we demonstrate how Escherichia coli tRNALysUUU with hypermodified 5-methylaminomethyl-2-thiouridine (mnm5s2U) at the wobble position discriminates between cognate codons AAA and AAG, and near-cognate stop codon UAA or isoleucine codon AUA, with which it forms pyrimidine–pyrimidine mismatches. We show that mnm5s2U forms an unusual pair with guanosine at the wobble position that expands general knowledge on the degeneracy of the genetic code and specifies a powerful role of tRNA modifications in translation. Our models consolidate the translational fidelity mechanism proposed previously where the steric complementarity and shape acceptance dominate the decoding mechanism.

Date: 2016
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DOI: 10.1038/ncomms10457

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