Evidence map›Paper›PMID 27159451›Full record

ArticleeLife2016

Structural characterization of ribosome recruitment and translocation by type IV IRES.

Jason Murray, Christos G Savva, Byung-Sik Shin, Thomas E Dever, V Ramakrishnan, Israel S Fernández

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing 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

69 citing papers in PubMed, 108 citations in OpenAlex.

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9 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

6 authors at 2 institutions in 2 countries.

Jason MurrayMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Christos G SavvaMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0003-3354-6483
Byung-Sik ShinLaboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, United States.
Thomas E DeverLaboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, United States.
V RamakrishnanMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Israel S FernándezMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0001-7218-1603
MRC Laboratory of Molecular Biology · GBNational Institutes of Health · US

Funding

Mechanism and Regulation of Eukaryotic Protein SynthesisZIAHD001010 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI DEVER, THOMAS E · 2009 to 2025
$29.4M
Medical Research Council MC_U105184332Wellcome Trust WT096570
6 · The paper itself

Abstract

Viral mRNA sequences with a type IV IRES are able to initiate translation without any host initiation factors. Initial recruitment of the small ribosomal subunit as well as two translocation steps before the first peptidyl transfer are essential for the initiation of translation by these mRNAs. Using electron cryomicroscopy (cryo-EM) we have structurally characterized at high resolution how the Cricket Paralysis Virus Internal Ribosomal Entry Site (CrPV-IRES) binds the small ribosomal subunit (40S) and the translocation intermediate stabilized by elongation factor 2 (eEF2). The CrPV-IRES restricts tvhe otherwise flexible 40S head to a conformation compatible with binding the large ribosomal subunit (60S). Once the 60S is recruited, the binary CrPV-IRES/80S complex oscillates between canonical and rotated states (Fernández et al., 2014; Koh et al., 2014), as seen for pre-translocation complexes with tRNAs. Elongation factor eEF2 with a GTP analog stabilizes the ribosome-IRES complex in a rotated state with an extra ~3 degrees of rotation. Key residues in domain IV of eEF2 interact with pseudoknot I (PKI) of the CrPV-IRES stabilizing it in a conformation reminiscent of a hybrid tRNA state. The structure explains how diphthamide, a eukaryotic and archaeal specific post-translational modification of a histidine residue of eEF2, is involved in translocation.

Indexed as

Internal Ribosome Entry SitesPeptide Chain Initiation, TranslationalCryoelectron MicroscopyDicistroviridaeKluyveromycesMacromolecular SubstancesPeptide Elongation Factor 2Ribosome Subunits, Small, EukaryoticRNA, MessengerRNA, ViralInternal Ribosome Entry SitesMacromolecular SubstancesPeptide Elongation Factor 2RNA, MessengerRNA, ViralbiochemistrybiophysicscricketIRESparalysisribosomeS. cerevisiaestructural biologytranslocationvirus infection

Identifiers

PMID27159451
PMCPMC4861600
OpenAlexW2345859988

What OpenQuestion holds

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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.