ArticleNature structural & molecular biology2015
Translational arrest by a prokaryotic signal recognition particle is mediated by RNA interactions.
Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 33 citations in OpenAlex.
- A B1 SINE element within the mouseScience advances · 2026Article
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025Review
- Cryo-EM structure of SRP68/72 reveals an extended dimerization domain with RNA-binding activity.Nucleic acids research · 2024Article
- A linear and circular dual-conformation noncoding RNA involved in oxidative stress tolerance in Bacillus altitudinis.Nature communications · 2023Article
- The dynamic architecture of Map1- and NatB-ribosome complexes coordinates the sequential modifications of nascent polypeptide chains.PLoS biology · 2023Article
- The translating bacterial ribosome at 1.55 Å resolution generated by cryo-EM imaging services.Nature communications · 2023Article
- Biophysical characterisation of human LincRNA-p21 sense and antisense Alu inverted repeats.Nucleic acids research · 2022Article
- Ribosome-Associated ncRNAs (rancRNAs) Adjust Translation and Shape Proteomes.Non-coding RNA · 2022Review
- Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp.Nature communications · 2022Article
- Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation.Communications biology · 2021Article
- How Quality Control Systems AID Sec-Dependent Protein Translocation.Frontiers in molecular biosciences · 2021Review
- Mechanism of ribosome shutdown by RsfS in Staphylococcus aureus revealed by integrative structural biology approach.Nature communications · 2020Article
- Co-Translational Protein Folding and Sorting in Chloroplasts.Plants (Basel, Switzerland) · 2020Review
- A Novel Noncoding RNABiomolecules · 2019Article
- sRNA OsiA Stabilizes Catalase mRNA during Oxidative Stress Response ofMicroorganisms · 2019Article
- A molecular recognition feature mediates ribosome-induced SRP-receptor assembly during protein targeting.The Journal of cell biology · 2019Article
- Protein Transport Across the Bacterial Plasma Membrane by the Sec Pathway.The protein journal · 2019Review
- Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome.Nature communications · 2017Article
- The nucleoside analog clitocine is a potent and efficacious readthrough agent.RNA (New York, N.Y.) · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The signal recognition particle (SRP) recognizes signal sequences of nascent polypeptides and targets ribosome-nascent chain complexes to membrane translocation sites. In eukaryotes, translating ribosomes are slowed down by the Alu domain of SRP to allow efficient targeting. In prokaryotes, however, little is known about the structure and function of Alu domain-containing SRPs. Here, we report a complete molecular model of SRP from the Gram-positive bacterium Bacillus subtilis, based on cryo-EM. The SRP comprises two subunits, 6S RNA and SRP54 or Ffh, and it facilitates elongation slowdown similarly to its eukaryotic counterpart. However, protein contacts with the small ribosomal subunit observed for the mammalian Alu domain are substituted in bacteria by RNA-RNA interactions of 6S RNA with the α-sarcin-ricin loop and helices H43 and H44 of 23S rRNA. Our findings provide a structural basis for cotranslational targeting and RNA-driven elongation arrest in prokaryotes.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.