Evidence map›Paper›PMID 25601755›Full record

ArticleMolecular cell2015

Cryo-EM of ribosomal 80S complexes with termination factors reveals the translocated cricket paralysis virus IRES.

Margarita Muhs, Tarek Hilal, Thorsten Mielke, Maxim A Skabkin, Karissa Y Sanbonmatsu, Tatyana V Pestova, Christian M T Spahn

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
7.2field-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

66 citing papers in PubMed, 101 citations in OpenAlex.

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6 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

7 authors at 4 institutions in 2 countries.

Margarita MuhsInstitut für Medizinische Physik und Biophysik, Charite - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany.
Tarek HilalInstitut für Medizinische Physik und Biophysik, Charite - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany.
Thorsten MielkeInstitut für Medizinische Physik und Biophysik, Charite - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany; UltraStrukturNetzwerk, Max Planck Institute for Molecular Genetics, 14195 Berlin, Germany.
Maxim A SkabkinDepartment of Cell Biology, SUNY Downstate Medical Center, Brooklyn, NY 11203, USA.
Karissa Y SanbonmatsuTheoretical Biology and Biophysics Group, Theoretical Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA; New Mexico Consortium, 4200 West Jemez Road, Suite 301, Los Alamos, NM 87544, USA.
Tatyana V PestovaDepartment of Cell Biology, SUNY Downstate Medical Center, Brooklyn, NY 11203, USA.
Christian M T SpahnInstitut für Medizinische Physik und Biophysik, Charite - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany. Electronic address: christian.spahn@charite.de.
Charité - Universitätsmedizin Berlin · DESUNY Downstate Health Sciences University · USLos Alamos National Laboratory · USMax Planck Institute for Molecular Genetics · DE

Funding

Large-Scale Simulations of Ribosomal DecodingR01GM072686 · NIGMS · UNIVERSITY OF CALIF-LOS ALAMOS NAT LAB · PI SANBONMATSU, KARISSA Y · 2005 to 2024
$5.5M
THE MECHANISMS OF EUKARYOTIC TRANSLATION TERMINATION AND RIBOSOMAL RECYCLINGR01GM080623 · NIGMS · SUNY DOWNSTATE MEDICAL CENTER · PI PESTOVA, TATYANA V · 2007 to 2015
$2.7M
NIGMS NIH HHS GM80623NIGMS NIH HHS R01 GM072686NIGMS NIH HHS R01 GM080623
6 · The paper itself

Abstract

The cricket paralysis virus (CrPV) uses an internal ribosomal entry site (IRES) to hijack the ribosome. In a remarkable RNA-based mechanism involving neither initiation factor nor initiator tRNA, the CrPV IRES jumpstarts translation in the elongation phase from the ribosomal A site. Here, we present cryoelectron microscopy (cryo-EM) maps of 80S⋅CrPV-STOP ⋅ eRF1 ⋅ eRF3 ⋅ GMPPNP and 80S⋅CrPV-STOP ⋅ eRF1 complexes, revealing a previously unseen binding state of the IRES and directly rationalizing that an eEF2-dependent translocation of the IRES is required to allow the first A-site occupation. During this unusual translocation event, the IRES undergoes a pronounced conformational change to a more stretched conformation. At the same time, our structural analysis provides information about the binding modes of eRF1 ⋅ eRF3 ⋅ GMPPNP and eRF1 in a minimal system. It shows that neither eRF3 nor ABCE1 are required for the active conformation of eRF1 at the intersection between eukaryotic termination and recycling.

Indexed as

ATP-Binding Cassette TransportersCryoelectron MicroscopyDicistroviridaeEukaryotic Initiation FactorsModels, MolecularMolecular ConformationMolecular Sequence DataNucleic Acid ConformationPeptide Termination FactorsProtein BiosynthesisRibosomesRNA, MessengerRNA, TransferRNA, ViralATP-Binding Cassette TransportersEukaryotic Initiation FactorsPeptide Termination FactorsRNA, MessengerRNA, TransferRNA, Viral

Identifiers

PMID25601755
PMCPMC4526138
OpenAlexW2085063254

What OpenQuestion holds

Textmetadata
LicenceTDM
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.