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

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 and Joachim Frank ()
Additional contact information
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

Nature Communications, 2013, vol. 4, issue 1, 1-8

Abstract: 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.

Date: 2013
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DOI: 10.1038/ncomms2470

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