Evidence map›Paper›PMID 26158507›Full record

ArticleeLife2015

Structures of the scanning and engaged states of the mammalian SRP-ribosome complex.

Rebecca M Voorhees, Ramanujan S Hegde

Abstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
–field-weighted citation impact
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

91 citing papers in PubMed.

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  19. High-resolution reconstruction of aRNA (New York, N.Y.) · 2024
    Article
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31 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Rebecca M VoorheesMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Ramanujan S HegdeMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.

Funding

Medical Research Council MC_UP_A022_1007Wellcome Trust
6 · The paper itself

Abstract

The universally conserved signal recognition particle (SRP) is essential for the biogenesis of most integral membrane proteins. SRP scans the nascent chains of translating ribosomes, preferentially engaging those with hydrophobic targeting signals, and delivers these ribosome-nascent chain complexes to the membrane. Here, we present structures of native mammalian SRP-ribosome complexes in the scanning and engaged states. These structures reveal the near-identical SRP architecture of these two states, show many of the SRP-ribosome interactions at atomic resolution, and suggest how the polypeptide-binding M domain selectively engages hydrophobic signals. The scanning M domain, pre-positioned at the ribosomal exit tunnel, is auto-inhibited by a C-terminal amphipathic helix occluding its hydrophobic binding groove. Upon engagement, the hydrophobic targeting signal displaces this amphipathic helix, which then acts as a protective lid over the signal. Biochemical experiments suggest how scanning and engagement are coordinated with translation elongation to minimize exposure of hydrophobic signals during membrane targeting.

Indexed as

Protein BiosynthesisAnimalsCryoelectron MicroscopyCrystallography, X-RayMacromolecular SubstancesMammalsModels, MolecularRibosomesSignal Recognition ParticleMacromolecular SubstancesSignal Recognition Particlebiochemistrybiophysicscryo-EMmembrane protein biogenesisprotein targetingrabbitsignal recognition particlestructural biology

Identifiers

PMID26158507
PMCPMC4497383

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Registered trials

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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.