Evidence map›Paper›PMID 29149347›Full record

ArticleNucleic acids research2017

Signal recognition particle binds to translating ribosomes before emergence of a signal anchor sequence.

Evan Mercier, Wolf Holtkamp, Marina V Rodnina, Wolfgang Wintermeyer

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 14% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. Translational landscape during seed germination revealed by ribosome profiling.The Plant journal : for cell and molecular biology · 2026
    Article
  4. Article
  5. Article
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  7. Spatiotemporal kinetics of the SRP pathway in liveProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Improved activity and expression of recombinant human factor IX by propeptide engineering.Daru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences · 2019
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Sequential activation of human signal recognition particle by the ribosome and signal sequence drives efficient protein targeting.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Evan MercierDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen 37077, Germany.
Wolf HoltkampDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen 37077, Germany.
Marina V RodninaDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen 37077, Germany.
Wolfgang WintermeyerDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen 37077, Germany.
Max Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bacterial signal recognition particle (SRP) is part of the machinery that targets ribosomes synthesizing membrane proteins to membrane-embedded translocons co-translationally. Recognition of nascent membrane proteins occurs by virtue of a hydrophobic signal-anchor sequence (SAS) contained in the nascent chain, usually at the N terminus. Here we use fluorescence-based stopped-flow to monitor SRP-ribosome interactions with actively translating ribosomes while an SRP substrate is synthesized and emerges from the peptide exit tunnel. The kinetic analysis reveals that, at cellular concentrations of ribosomes and SRP, SRP rapidly binds to translating ribosomes prior to the emergence of an SAS and forms an initial complex that rapidly rearranges to a more stable engaged complex. When the growing peptide reaches a length of ∼50 amino acids and the SAS is partially exposed, SRP undergoes another conformational change which further stabilizes the complex and initiates targeting of the translating ribosome to the translocon. These results provide a reconciled view on the timing of high-affinity targeting complex formation, while emphasizing the existence of preceding SRP recruitment steps under conditions of ongoing translation.

Indexed as

Protein BiosynthesisProtein Sorting SignalsEscherichia coliEscherichia coli ProteinsKineticsModels, MolecularProtein BindingProtein ConformationRibosomesSignal Recognition ParticleTime FactorsEscherichia coli ProteinsFfh protein, E coliProtein Sorting SignalsSignal Recognition Particle

Identifiers

PMID29149347
PMCPMC5714171
OpenAlexW2762974646

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.