Journal
MOLECULAR CELL
Volume 22, Issue 5, Pages 587-598Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2006.05.021
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Funding
- Intramural NIH HHS Funding Source: Medline
- NIGMS NIH HHS [GM26494] Funding Source: Medline
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When the export of E. coli Sects is blocked, a 17 amino acid motif near the C terminus of the protein induces a translation arrest from within the ribosome tunnel. Here we used a recently described application of fluorescence resonance energy transfer (FRET) to gain insight into the mechanism of translation arrest. We found that the Sects C terminus adopted a compact conformation upon synthesis of the arrest motif. This conformational change did not occur spontaneously, but rather was induced by the ribosome. Translation arrest required both compaction of the Sects C terminus and the presence of key residues in the arrest motif. Further analysis showed that the arrested peptidyl-tRNA was resistant to puromycin treatment and revealed additional changes in the ribosome-nascent Sects complex. Based on these observations, we propose that translation arrest results from a series of reciprocal interactions between the ribosome and the C terminus of the nascent Sects polypeptide.
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