Evidence map›Paper›PMID 28683310›Full record

ArticleCell reports2017

Post-termination Ribosome Intermediate Acts as the Gateway to Ribosome Recycling.

Arjun Prabhakar, Mark C Capece, Alexey Petrov, Junhong Choi, Joseph D Puglisi

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. A cascade of structural rearrangements positions peptide release factor 2 for polypeptide hydrolysis on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

5 authors at 1 institution in 1 country.

Arjun PrabhakarDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA; Program in Biophysics, Stanford University, Stanford, CA 94305, USA.
Mark C CapeceDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA; Department of Chemistry, Stanford University, Stanford, CA 94305, USA.
Alexey PetrovDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Junhong ChoiDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA; Department of Applied Physics, Stanford University, Stanford, CA 94305, USA.
Joseph D PuglisiDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA. Electronic address: puglisi@stanford.edu.
Stanford University · US

Funding

STRUCTURAL BASIS FOR RIBOSOME FUNCTIONSR01GM051266 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI PUGLISI, JOSEPH D · 1995 to 2021
$7.7M
Molecular Biophysics Training Program at StanfordT32GM008294 · NIGMS · STANFORD UNIVERSITY · PI HUANG, KERWYN C. · 1989 to 2019
$7.4M
Single molecule translational profilingR01GM099687 · NIGMS · STANFORD UNIVERSITY · PI PUGLISI, JOSEPH D · 2011 to 2015
$4.3M
NIGMS NIH HHS R01 GM051266NIGMS NIH HHS R01 GM099687NIGMS NIH HHS T32 GM008294
6 · The paper itself

Abstract

During termination of translation, the nascent peptide is first released from the ribosome, which must be subsequently disassembled into subunits in a process known as ribosome recycling. In bacteria, termination and recycling are mediated by the translation factors RF, RRF, EF-G, and IF3, but their precise roles have remained unclear. Here, we use single-molecule fluorescence to track the conformation and composition of the ribosome in real time during termination and recycling. Our results show that peptide release by RF induces a rotated ribosomal conformation. RRF binds to this rotated intermediate to form the substrate for EF-G that, in turn, catalyzes GTP-dependent subunit disassembly. After the 50S subunit departs, IF3 releases the deacylated tRNA from the 30S subunit, thus preventing reassembly of the 70S ribosome. Our findings reveal the post-termination rotated state as the crucial intermediate in the transition from termination to recycling.

Indexed as

Peptide Chain Termination, TranslationalEscherichia coliEscherichia coli ProteinsRibosomal ProteinsRibosome Subunits, Large, BacterialEscherichia coli ProteinsRibosomal ProteinsEF-GIF3recyclingrelease factorribosomeRRFsingle-molecule fluorescencestop codonterminationtranslation

Identifiers

PMID28683310
PMCPMC5555083
OpenAlexW2726749510

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.