Evidence map›Paper›PMID 26804923›Full record

ArticleNature communications2016

Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon.

Ahmad Jomaa, Daniel Boehringer, Marc Leibundgut, Nenad Ban

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
9.7field-weighted citation impact, top 2% 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

67 citing papers in PubMed, 107 citations in OpenAlex.

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  10. Cells · 2024
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  16. Spatiotemporal kinetics of the SRP pathway in liveProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Article
  18. Article
  19. Article
  20. Review

7 more citing papers are in PubMed but not listed here.

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.

Ahmad JomaaDepartment of Biology, Institute of Molecular Biology and Biophysics, Otto-Stern-Weg 5, ETH Zurich CH-8093, Switzerland.
Daniel BoehringerDepartment of Biology, Institute of Molecular Biology and Biophysics, Otto-Stern-Weg 5, ETH Zurich CH-8093, Switzerland.
Marc LeibundgutDepartment of Biology, Institute of Molecular Biology and Biophysics, Otto-Stern-Weg 5, ETH Zurich CH-8093, Switzerland.
Nenad BanDepartment of Biology, Institute of Molecular Biology and Biophysics, Otto-Stern-Weg 5, ETH Zurich CH-8093, Switzerland.
ETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Co-translational protein targeting to membranes is a universally conserved process. Central steps include cargo recognition by the signal recognition particle and handover to the Sec translocon. Here we present snapshots of key co-translational-targeting complexes solved by cryo-electron microscopy at near-atomic resolution, establishing the molecular contacts between the Escherichia coli translating ribosome, the signal recognition particle and the translocon. Our results reveal the conformational changes that regulate the latching of the signal sequence, the release of the heterodimeric domains of the signal recognition particle and its receptor, and the handover of the signal sequence to the translocon. We also observe that the signal recognition particle and the translocon insert-specific structural elements into the ribosomal tunnel to remodel it, possibly to sense nascent chains. Our work provides structural evidence for a conformational state of the signal recognition particle and its receptor primed for translocon binding to the ribosome-nascent chain complex.

Indexed as

CodonCryoelectron MicroscopyEscherichia coliEscherichia coli ProteinsModels, MolecularProtein BindingProtein BiosynthesisProtein TransportReceptors, Cytoplasmic and NuclearReceptors, PeptideRibosomesRNA, MessengerSignal Recognition ParticleTranscription FactorsCodonEscherichia coli ProteinsReceptors, Cytoplasmic and NuclearReceptors, PeptideRNA, MessengerSecM protein, E colisignal peptide receptorSignal Recognition ParticleTranscription Factors

Identifiers

PMID26804923
PMCPMC4737761
OpenAlexW2264866006

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.