Evidence map›Paper›PMID 28542628›Full record

ArticlePloS one2017

Chemical and structural characterization of a model Post-Termination Complex (PoTC) for the ribosome recycling reaction: Evidence for the release of the mRNA by RRF and EF-G.

Nobuhiro Iwakura, Takeshi Yokoyama, Fabio Quaglia, Kaoru Mitsuoka, Kazuhiro Mio, Hideki Shigematsu, Mikako Shirouzu, Akira Kaji, Hideko Kaji

Abstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Structural basis for ribosome recycling by RRF and tRNA.Nature structural & molecular biology · 2020
    Article
  5. Article
  6. Disassembly of theProceedings of the National Academy of Sciences of the United States of America · 2017
    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

9 authors.

Nobuhiro IwakuraDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Jefferson Medical College, Philadelphia, Pennsylvania, United States of America.
Takeshi YokoyamaDivision of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, Yokohama, Japan.
Fabio QuagliaDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Jefferson Medical College, Philadelphia, Pennsylvania, United States of America.
Kaoru MitsuokaResearch Center for Ultra-High Voltage Electron Microscopy, Osaka University, Osaka, Japan.
Kazuhiro MioMolecular Profiling Research Center for Drug Discovery and OPERANDO Open Innovation Laboratory, National Institute of Advanced Industrial Science and Technology, Tokyo, Japan.
Hideki ShigematsuDivision of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, Yokohama, Japan.
Mikako ShirouzuDivision of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, Yokohama, Japan.
Akira KajiDepartment of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America.
Hideko KajiDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Jefferson Medical College, Philadelphia, Pennsylvania, United States of America.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A model Post-Termination Complex (PoTC) used for the discovery of Ribosome Recycling Factor (RRF) was purified and characterized by cryo-electron microscopic analysis and biochemical methods. We established that the model PoTC has mostly one tRNA, at the P/E or P/P position, together with one mRNA. The structural studies were supported by the biochemical measurement of bound tRNA and mRNA. Using this substrate, we establish that the release of tRNA, release of mRNA and splitting of ribosomal subunits occur during the recycling reaction. Order of these events is tRNA release first followed by mRNA release and splitting almost simultaneously. Moreover, we demonstrate that IF3 is not involved in any of the recycling reactions but simply prevents the re-association of split ribosomal subunits. Our finding demonstrates that the important function of RRF includes the release of mRNA, which is often missed by the use of a short ORF with the Shine-Dalgarno sequence near the termination site.

Indexed as

Cryoelectron MicroscopyEscherichia coliPeptide Chain Termination, TranslationalPeptide Elongation Factor GPeptide Termination FactorsProkaryotic Initiation Factor-3Ribosomal ProteinsRibosomesRNA, MessengerRNA, TransferPeptide Elongation Factor GPeptide Termination FactorsProkaryotic Initiation Factor-3Ribosomal Proteinsribosome releasing factorRNA, MessengerRNA, Transfer

Identifiers

PMID28542628
PMCPMC5443523

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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.