ArticleNucleic acids research2021
Search for translation arrest peptides encoded upstream of genes for components of protein localization pathways.
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 12 papers.
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Who cites it
12 citing papers in PubMed.
- Structural insights into YheS-mediated release of SecM-arrested ribosome.Nature communications · 2026Article
- Diverse mechanisms of translation arrest by a Clostridia ribosome stalling peptide CliM.Nature communications · 2026Article
- Evolutionary adaptation of bacterial proteomes to translation-impeding sequences.The EMBO journal · 2026Article
- Structural basis of enhanced stalling efficiency of an engineered ribosome arrest peptide.Nucleic acids research · 2025Article
- A mini-hairpin shaped nascent peptide blocks translation termination by a distinct mechanism.Nature communications · 2025Article
- A role for the S4-domain containing protein YlmH in ribosome-associated quality control in Bacillus subtilis.Nucleic acids research · 2024Article
- The ABCF proteins in Escherichia coli individually cope with 'hard-to-translate' nascent peptide sequences.Nucleic acids research · 2024Article
- Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery.Nature communications · 2024Article
- RAPP-containing arrest peptides induce translational stalling by short circuiting the ribosomal peptidyltransferase activity.Nature communications · 2024Article
- The SecM arrest peptide traps a pre-peptide bond formation state of the ribosome.Nature communications · 2024Article
- B. subtilis MutS2 splits stalled ribosomes into subunits without mRNA cleavage.The EMBO journal · 2024Article
- Geometric differences in the ribosome exit tunnel impact the escape of small nascent proteins.Biophysical journal · 2023Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Regulatory nascent peptides participate in the regulation of cellular functions by the mechanisms involving regulated translation arrest. A class of them in bacteria, called monitoring substrates, feedback-regulates the expression of a specific component of protein localization machinery. Three monitoring substrates, SecM, MifM and VemP have previously been identified. Here, we attempt at identifying additional arrest peptides in bacteria. Our bioinformatic searches over more than 400 bacterial genomic sequences for proteins that have the common characteristic features shared by the known monitoring substrates and subsequent in vitro and in vivo characterization of the highlighted sequences allowed the identification of three arrest peptides termed ApcA, ApdA and ApdP. ApcA and ApdA homologs are conserved among a subset of actinobacteria, whereas ApdP has homologs in a subset of α-proteobacteria. We demonstrate that these arrest peptides, in their ribosome-tethered nascent states, inhibit peptidyl transfer. The elongation arrest occurs at a specific codon near the 3' end of the coding region, in a manner depending on the amino acid sequence of the nascent chain. Interestingly, the arrest sequences of ApcA, ApdA and ApdP share a sequence R-A-P-G/P that is essential for the elongation arrest.
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