Translation Arrest Requires Two-Way Communication between a Nascent Polypeptide and the Ribosome
- Resource Type
- Authors
- Cheryl A. Woolhead; Arthur E. Johnson; Harris D. Bernstein
- Source
- Molecular Cell. 22:587-598
- Subject
- Conformational change
Protein Conformation
Amino Acid Motifs
Molecular Sequence Data
Peptide Chain Elongation, Translational
Biology
Models, Biological
Ribosome
chemistry.chemical_compound
Fluorescence Resonance Energy Transfer
Amino Acid Sequence
Molecular Biology
Fluorescent Dyes
Amino acid motif
Escherichia coli Proteins
C-terminus
RNA
Gene Expression Regulation, Bacterial
Cell Biology
Förster resonance energy transfer
chemistry
Biochemistry
Puromycin
Mutation
Biophysics
Peptides
Ribosomes
Transcription Factors
- Language
- ISSN
- 1097-2765
When the export of E. coli SecM 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 SecM 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 SecM 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 SecM 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 SecM polypeptide.