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Mechanism of tetracycline resistance by ribosomal protection protein Tet(O)

Author

Listed:
  • Wen Li

    (Columbia University)

  • Gemma C. Atkinson

    (Institute of Technology, University of Tartu)

  • Nehal S. Thakor

    (Apoptosis Research Centre, University of Ottawa)

  • Ülar Allas

    (Institute of Technology, University of Tartu)

  • Chuao-chao Lu

    (Beijing University)

  • Kwok-Yan Chan

    (University of Illinois at Urbana-Champaign)

  • Tanel Tenson

    (Institute of Technology, University of Tartu)

  • Klaus Schulten

    (University of Illinois at Urbana-Champaign)

  • Kevin S. Wilson

    (Oklahoma State University)

  • Vasili Hauryliuk

    (Institute of Technology, University of Tartu)

  • Joachim Frank

    (Columbia University
    Howard Hughes Medical Institute, Columbia University
    Columbia University)

Abstract

Tetracycline resistance protein Tet(O), which protects the bacterial ribosome from binding the antibiotic tetracycline, is a translational GTPase with significant similarity in both sequence and structure to the elongation factor EF-G. Here, we present an atomic model of the Tet(O)-bound 70S ribosome based on our cryo-electron microscopic reconstruction at 9.6-Å resolution. This atomic model allowed us to identify the Tet(O)-ribosome binding sites, which involve three characteristic loops in domain 4 of Tet(O). Replacements of the three amino-acid tips of these loops by a single glycine residue result in loss of Tet(O)-mediated tetracycline resistance. On the basis of these findings, the mechanism of Tet(O)-mediated tetracycline resistance can be explained in molecular detail.

Suggested Citation

  • Wen Li & Gemma C. Atkinson & Nehal S. Thakor & Ülar Allas & Chuao-chao Lu & Kwok-Yan Chan & Tanel Tenson & Klaus Schulten & Kevin S. Wilson & Vasili Hauryliuk & Joachim Frank, 2013. "Mechanism of tetracycline resistance by ribosomal protection protein Tet(O)," Nature Communications, Nature, vol. 4(1), pages 1-8, June.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2470
    DOI: 10.1038/ncomms2470
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