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

Author

Listed:
  • Alexey Rozov

    (Institute of Genetics and Molecular and Cellular Biology, INSERM, U964; CNRS/University of Strasbourg
    CNRS/University of Strasbourg)

  • Natalia Demeshkina

    (Institute of Genetics and Molecular and Cellular Biology, INSERM, U964; CNRS/University of Strasbourg
    CNRS/University of Strasbourg)

  • Iskander Khusainov

    (Institute of Genetics and Molecular and Cellular Biology, INSERM, U964; CNRS/University of Strasbourg
    CNRS/University of Strasbourg
    Institute of Fundamental Medicine and Biology, Kazan Federal University)

  • 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
    CNRS/University of Strasbourg)

  • Gulnara Yusupova

    (Institute of Genetics and Molecular and Cellular Biology, INSERM, U964; CNRS/University of Strasbourg
    CNRS/University of Strasbourg)

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.

Suggested Citation

  • Alexey Rozov & Natalia Demeshkina & Iskander Khusainov & Eric Westhof & Marat Yusupov & Gulnara Yusupova, 2016. "Novel base-pairing interactions at the tRNA wobble position crucial for accurate reading of the genetic code," Nature Communications, Nature, vol. 7(1), pages 1-10, April.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10457
    DOI: 10.1038/ncomms10457
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    Cited by:

    1. Caillan Crowe-McAuliffe & Victoriia Murina & Kathryn Jane Turnbull & Susanne Huch & Marje Kasari & Hiraku Takada & Lilit Nersisyan & Arnfinn Sundsfjord & Kristin Hegstad & Gemma C. Atkinson & Vicent P, 2022. "Structural basis for PoxtA-mediated resistance to phenicol and oxazolidinone antibiotics," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    2. Markus Hillmeier & Mirko Wagner & Timm Ensfelder & Eva Korytiakova & Peter Thumbs & Markus Müller & Thomas Carell, 2021. "Synthesis and structure elucidation of the human tRNA nucleoside mannosyl-queuosine," Nature Communications, Nature, vol. 12(1), pages 1-9, December.
    3. Dylan Girodat & Hans-Joachim Wieden & Scott C. Blanchard & Karissa Y. Sanbonmatsu, 2023. "Geometric alignment of aminoacyl-tRNA relative to catalytic centers of the ribosome underpins accurate mRNA decoding," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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