ArticleNature communications2024
The SecM arrest peptide traps a pre-peptide bond formation state of the ribosome.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Quasi-continuous cotranslational compaction and folding of a multidomain protein.Nature communications · 2026Article
- Substrate-induced assembly and functional mechanism of the membrane protein insertase SecYEG-YidC.The EMBO journal · 2026Article
- Cotranslational Folding and "Constrained Monomers" in the Maturation of HIV-1 Protease.Journal of molecular biology · 2026Article
- A family of archaeal hibernation factors that bind in tandem and protect ribosomes in dormant cells.Nature communications · 2026Article
- RATEX: A Scalable RNA-Based Platform for Logical and Multi-Layered Cellular Programming.Angewandte Chemie (International ed. in English) · 2026Article
- Structural insights into YheS-mediated release of SecM-arrested ribosome.Nature communications · 2026Article
- Article
- Diverse mechanisms of translation arrest by a Clostridia ribosome stalling peptide CliM.Nature communications · 2026Article
- Hydrogen/deuterium exchange mass spectrometry analysis of ribosome-nascent chain complexes to study protein biogenesis at the peptide level.Nature protocols · 2026Article
- Mechanism of ribosome stalling by the AMD1 C-terminal tail arrest peptide.Science advances · 2026Article
- Evolutionary adaptation of bacterial proteomes to translation-impeding sequences.The EMBO journal · 2026Article
- Structural modification of oxazolidinone antibiotics alters nascent peptide stalling preference and peptide trajectory through the ribosome.bioRxiv : the preprint server for biology · 2026Article
- Quasi-continuous cotranslational compaction and folding of a multidomain protein.bioRxiv : the preprint server for biology · 2026Article
- Constant trouble with prolines-navigating a global translation dilemma.Nucleic acids research · 2026Review
- SARS-CoV-2 membrane protein biogenesis.bioRxiv : the preprint server for biology · 2026Article
- A family of archaeal hibernation factors that bind in tandem and protect ribosomes in dormant cells.bioRxiv : the preprint server for biology · 2026Article
- The human ribosome modulates multidomain protein biogenesis by delaying cotranslational domain docking.Nature structural & molecular biology · 2025Article
- Structural basis of enhanced stalling efficiency of an engineered ribosome arrest peptide.Nucleic acids research · 2025Article
- Are Bacterial Processes Dependent on Global Ribosome Pausing Affected by tRNA Modification Defects?Journal of molecular biology · 2025Review
- Cotranslational membrane insertion of the voltage-sensitive KProceedings of the National Academy of Sciences of the United States of America · 2025Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors.
Funding
Abstract
Nascent polypeptide chains can induce translational stalling to regulate gene expression. This is exemplified by the E. coli secretion monitor (SecM) arrest peptide that induces translational stalling to regulate expression of the downstream encoded SecA, an ATPase that co-operates with the SecYEG translocon to facilitate insertion of proteins into or through the cytoplasmic membrane. Here we present the structure of a ribosome stalled during translation of the full-length E. coli SecM arrest peptide at 2.0 Å resolution. The structure reveals that SecM arrests translation by stabilizing the Pro-tRNA in the A-site, but in a manner that prevents peptide bond formation with the SecM-peptidyl-tRNA in the P-site. By employing molecular dynamic simulations, we also provide insight into how a pulling force on the SecM nascent chain can relieve the SecM-mediated translation arrest. Collectively, the mechanisms determined here for SecM arrest and relief are also likely to be applicable for a variety of other arrest peptides that regulate components of the protein localization machinery identified across a wide range of bacteria lineages.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.