Evidence map›Paper›PMID 23755360›Full record

ArticleeLife2013

Cryo-EM visualization of the ribosome in termination complex with apo-RF3 and RF1.

Jesper Pallesen, Yaser Hashem, Gürkan Korkmaz, Ravi Kiran Koripella, Chenhui Huang, Måns Ehrenberg, Suparna Sanyal, Joachim Frank

Open access · goldAbstract readVideo-Audio Media
In one paragraph

Article in eLife, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

25 citing papers in PubMed, 40 citations in OpenAlex.

  1. 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
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Joachim Frank's Binding with the Ribosome.Structure (London, England : 1993) · 2019
    Review
  13. Translation in Prokaryotes.Cold Spring Harbor perspectives in biology · 2018
    Review
  14. Article
  15. Article
  16. Article
  17. Complementary charge-based interaction between the ribosomal-stalk protein L7/12 and IF2 is the key to rapid subunit association.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Article
  19. Article
  20. 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

8 authors at 2 institutions in 2 countries.

Jesper PallesenDepartment of Biochemistry and Molecular Biophysics , Howard Hughes Medical Institute, Columbia University , New York City , United States.
Yaser Hashem
Gürkan Korkmaz
Ravi Kiran Koripella
Chenhui Huang
Måns Ehrenberg
Suparna Sanyal
Joachim Frank
Uppsala University · SEColumbia University · US

Funding

STRUCTURE ANALYSIS OF MACROMOLECULAR ASSEMBLIESR01GM029169 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1985 to 2019
$6.1M
NIGMS NIH HHS R01 GM029169
6 · The paper itself

Abstract

Termination of messenger RNA translation in Bacteria and Archaea is initiated by release factors (RFs) 1 or 2 recognizing a stop codon in the ribosomal A site and releasing the peptide from the P-site transfer RNA. After release, RF-dissociation is facilitated by the G-protein RF3. Structures of ribosomal complexes with RF1 or RF2 alone or with RF3 alone-RF3 bound to a non-hydrolyzable GTP-analog-have been reported. Here, we present the cryo-EM structure of a post-termination ribosome containing both apo-RF3 and RF1. The conformation of RF3 is distinct from those of free RF3•GDP and ribosome-bound RF3•GDP(C/N)P. Furthermore, the conformation of RF1 differs from those observed in RF3-lacking ribosomal complexes. Our study provides structural keys to the mechanism of guanine nucleotide exchange on RF3 and to an L12-mediated ribosomal recruitment of RF3. In conjunction with previous observations, our data provide the foundation to structurally characterize the complete action cycle of the G-protein RF3. DOI:http://dx.doi.org/10.7554/eLife.00411.001.

Indexed as

Cryoelectron MicroscopyTranscription Termination, GeneticBinding SitesEscherichia coli ProteinsGuanosine DiphosphateGuanosine TriphosphateMolecular Dynamics SimulationMutationPeptide Termination FactorsProtein BindingProtein ConformationRibosomal ProteinsRibosomesRNA, BacterialRNA, MessengerTime FactorsEscherichia coli ProteinsGuanosine DiphosphateGuanosine TriphosphatePeptide Termination FactorsprfA protein, E coliprfC protein, E coliRibosomal ProteinsRNA, BacterialRNA, MessengerrplL protein, E coliCryo-EME. coliL7/L12RF1RF3RibosomeStructure

Identifiers

PMID23755360
PMCPMC3677378
OpenAlexW2088327469

What OpenQuestion holds

Textmetadata
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.