Journal
SCIENCE
Volume 326, Issue 5958, Pages 1412-1415Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1177662
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Funding
- Deutsche Forschungsgemeinschaft [SFB594, SFB646, SFB740, WI3285/1-1]
- NIH [GM022778, P41-RR05969]
- NSF [PHY0822613, MCA93S028]
- European Union and Senatsverwaltung fur Wissenschaft
- Forschung und Kultur Berlin
- Direct For Mathematical & Physical Scien
- Division Of Physics [0822613] Funding Source: National Science Foundation
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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.
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