Structural insight into nascent polypeptide chain-mediated translational stalling

Birgit Seidelt, C. Axel Innis, Daniel N. Wilson, Marco Gartmann, Jean Paul Armache, Elizabeth Villa, Leonardo G. Trabuco, Thomas Becker, Thorsten Mielke, Klaus Schulten, Thomas A. Steitz, Roland Beckmann

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197 Scopus citations

Abstract

Expression of the Escherichia coli tryptophanase operon depends on ribosome stalling during translation of the upstream TnaC leader peptide, a process for which interactions between the TnaC nascent chain and the ribosomal exit tunnel are critical. We determined a 5.8 angstrom-resolution cryo-electron microscopy and single-particle reconstruction of a ribosome stalled during translation of the tnaC Leader gene. The nascent chain was extended within the exit tunnel, making contacts with ribosomal components at distinct sites. Upon stalling, two conserved residues within the peptidyltransferase center adopted conformations that preclude binding of release factors. We propose a model whereby interactions within the tunnel are relayed to the peptidyltransferase center to inhibit translation. Moreover, we show that nascent chains adopt distinct conformations within the ribosomal exit tunnel.

Original languageEnglish (US)
Pages (from-to)1412-1415
Number of pages4
JournalScience
Volume326
Issue number5958
DOIs
Publication statusPublished - Dec 4 2009

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All Science Journal Classification (ASJC) codes

  • General

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Seidelt, B., Innis, C. A., Wilson, D. N., Gartmann, M., Armache, J. P., Villa, E., ... Beckmann, R. (2009). Structural insight into nascent polypeptide chain-mediated translational stalling. Science, 326(5958), 1412-1415. https://doi.org/10.1126/science.1177662