ArticleNature communications2025
A mini-hairpin shaped nascent peptide blocks translation termination by a distinct mechanism.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Structural insights into YheS-mediated release of SecM-arrested ribosome.Nature communications · 2026Article
- Mechanism of ribosome stalling by the AMD1 C-terminal tail arrest peptide.Science advances · 2026Article
- Metabolic environment-driven remodeling of mitochondrial ribosomes regulates translation and biogenesis.Molecular cell · 2025Article
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Authors and funding
10 authors.
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Abstract
Protein synthesis by ribosomes produces functional proteins but also serves diverse regulatory functions, which depend on the coding amino acid sequences. Certain nascent peptides interact with the ribosome exit tunnel to arrest translation and modulate themselves or the expression of downstream genes. However, a comprehensive understanding of the mechanisms of such ribosome stalling and its regulation remains elusive. In this study, we systematically screen for unidentified ribosome arrest peptides through phenotypic evaluation, proteomics, and mass spectrometry analyses, leading to the discovery of the arrest peptides PepNL and NanCL in E. coli. Our cryo-EM study on PepNL reveals a distinct arrest mechanism, in which the N-terminus of PepNL folds back towards the tunnel entrance to prevent the catalytic GGQ motif of the release factor from accessing the peptidyl transferase center, causing translation arrest at the UGA stop codon. Furthermore, unlike sensory arrest peptides that require an arrest inducer, PepNL uses tryptophan as an arrest inhibitor, where Trp-tRNA
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