ArticleNucleic acids research2021
Structural basis of l-tryptophan-dependent inhibition of release factor 2 by the TnaC arrest peptide.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Diverse mechanisms of translation arrest by a Clostridia ribosome stalling peptide CliM.Nature communications · 2026Article
- Mechanism of ribosome stalling by the AMD1 C-terminal tail arrest peptide.Science advances · 2026Article
- A mini-hairpin shaped nascent peptide blocks translation termination by a distinct mechanism.Nature communications · 2025Article
- Single-residue effects on the behavior of a nascent polypeptide chain inside the ribosome exit tunnel.bioRxiv : the preprint server for biology · 2024Article
- Structural basis for differential inhibition of eukaryotic ribosomes by tigecycline.Nature communications · 2024Article
- AutoRNC: An automated modeling program for building atomic models of ribosome-nascent chain complexes.Structure (London, England : 1993) · 2024Article
- Mapping Protein-Protein Interactions at Birth: Single-Particle Cryo-EM Analysis of a Ribosome-Nascent Globin Complex.ACS central science · 2024Article
- B. subtilis MutS2 splits stalled ribosomes into subunits without mRNA cleavage.The EMBO journal · 2024Article
- Control of mRNA fate by its encoded nascent polypeptide.Molecular cell · 2023Review
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Authors and funding
9 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
In Escherichia coli, elevated levels of free l-tryptophan (l-Trp) promote translational arrest of the TnaC peptide by inhibiting its termination. However, the mechanism by which translation-termination by the UGA-specific decoding release factor 2 (RF2) is inhibited at the UGA stop codon of stalled TnaC-ribosome-nascent chain complexes has so far been ambiguous. This study presents cryo-EM structures for ribosomes stalled by TnaC in the absence and presence of RF2 at average resolutions of 2.9 and 3.5 Å, respectively. Stalled TnaC assumes a distinct conformation composed of two small α-helices that act together with residues in the peptide exit tunnel (PET) to coordinate a single L-Trp molecule. In addition, while the peptidyl-transferase center (PTC) is locked in a conformation that allows RF2 to adopt its canonical position in the ribosome, it prevents the conserved and catalytically essential GGQ motif of RF2 from adopting its active conformation in the PTC. This explains how translation of the TnaC peptide effectively allows the ribosome to function as a L-Trp-specific small-molecule sensor that regulates the tnaCAB operon.
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