Evidence map›Paper›PMID 27818103›Full record

ArticleStructure (London, England : 1993)2016

Key Intermediates in Ribosome Recycling Visualized by Time-Resolved Cryoelectron Microscopy.

Ziao Fu, Sandip Kaledhonkar, Anneli Borg, Ming Sun, Bo Chen, Robert A Grassucci, Måns Ehrenberg, Joachim Frank

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

43 citing papers in PubMed, 78 citations in OpenAlex.

  1. eLife · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Recent advances and current trends in cryo-electron microscopy.Current opinion in structural biology · 2022
    Review
  13. The Structural Dynamics of Translation.Annual review of biochemistry · 2022
    Review
  14. Review
  15. Review
  16. Challenges and approaches to studying pore-forming proteins.Biochemical Society transactions · 2021
    Review
  17. Review
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Ziao FuIntegrated Program in Cellular, Molecular, and Biomedical Studies, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.
Sandip KaledhonkarDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10027, USA.
Anneli BorgDepartment of Cell and Molecular Biology, Uppsala University, Uppsala 751 24, Sweden.
Ming SunDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Bo ChenDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Robert A GrassucciDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10027, USA; Howard Hughes Medical Institute, Columbia University, New York, NY 10032, USA.
Måns EhrenbergDepartment of Cell and Molecular Biology, Uppsala University, Uppsala 751 24, Sweden.
Joachim FrankDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10027, USA; Department of Biological Sciences, Columbia University, New York, NY 10027, USA; Howard Hughes Medical Institute, Columbia University, New York, NY 10032, USA. Electronic address: jf2192@cumc.columbia.edu.
Columbia University · USUppsala University · SEHoward Hughes Medical Institute · US

Funding

TRAINING IN CELLULAR, MOLECULAR AND BIOPHYSICAL STUDIEST32GM008224 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI LIEM, RONALD K. · 1987 to 2021
$9.9M
STRUCTURE ANALYSIS OF MACROMOLECULAR ASSEMBLIESR01GM029169 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1985 to 2019
$6.1M
Time-resolved Cryo-EM of Short-lived States in Eukaryotic TranslationR01GM055440 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1997 to 2020
$5.1M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM029169NIGMS NIH HHS R01 GM055440NIGMS NIH HHS T32 GM008224
6 · The paper itself

Abstract

Upon encountering a stop codon on mRNA, polypeptide synthesis on the ribosome is terminated by release factors, and the ribosome complex, still bound with mRNA and P-site-bound tRNA (post-termination complex, PostTC), is split into ribosomal subunits, ready for a new round of translational initiation. Separation of post-termination ribosomes into subunits, or "ribosome recycling," is promoted by the joint action of ribosome-recycling factor (RRF) and elongation factor G (EF-G) in a guanosine triphosphate (GTP) hydrolysis-dependent manner. Here we used a mixing-spraying-based method of time-resolved cryo-electron microscopy (cryo-EM) to visualize the short-lived intermediates of the recycling process. The two complexes that contain (1) both RRF and EF-G bound to the PostTC or (2) deacylated tRNA bound to the 30S subunit are of particular interest. Our observations of the native form of these complexes demonstrate the strong potential of time-resolved cryo-EM for visualizing previously unobservable transient structures.

Indexed as

Binding SitesCryoelectron MicroscopyEscherichia coliEscherichia coli ProteinsGuanosine TriphosphateModels, MolecularPeptide Elongation Factor GProtein BindingProtein BiosynthesisRibosomal ProteinsRibosomesRNA, TransferEscherichia coli ProteinsGuanosine TriphosphatePeptide Elongation Factor GRibosomal Proteinsribosome releasing factorRNA, Transfercryo-EMmixing-sprayingrecyclingribosometime-resolved

Identifiers

PMID27818103
PMCPMC5143168
OpenAlexW2548199696

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.