Evidence map›Paper›PMID 18234219›Full record

ArticleJournal of molecular biology2008

Structural Insights into ribosome recycling factor interactions with the 70S ribosome.

Raj D Pai, Wen Zhang, Barbara S Schuwirth, Go Hirokawa, Hideko Kaji, Akira Kaji, Jamie H D Cate

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Crystal structure of eukaryotic ribosome and its complexes with inhibitors.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Ribosome recycling step in yeast cytoplasmic protein synthesis is catalyzed by eEF3 and ATP.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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

7 authors at 3 institutions in 1 country.

Raj D PaiDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
Wen Zhang
Barbara S Schuwirth
Go Hirokawa
Hideko Kaji
Akira Kaji
Jamie H D Cate
University of California, Berkeley · USThomas Jefferson University · USUniversity of Pennsylvania · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
The Role of the Ribosome in the Accuracy of TranslationR01GM065050 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI CATE, JAMIE H · 2001 to 2022
$7.4M
RIBOSOME RECYCLING FACTOR(RRF) IN PROKARYOTESR01GM060429 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI KAJI, AKIRA · 2001 to 2004
$1.1M
NCI NIH HHS CA92584NCI NIH HHS P01 CA092584NIGMS NIH HHS GM60429NIGMS NIH HHS GM65050NIGMS NIH HHS R01 GM060429NIGMS NIH HHS R01 GM065050
6 · The paper itself

Abstract

At the end of translation in bacteria, ribosome recycling factor (RRF) is used together with elongation factor G to recycle the 30S and 50S ribosomal subunits for the next round of translation. In x-ray crystal structures of RRF with the Escherichia coli 70S ribosome, RRF binds to the large ribosomal subunit in the cleft that contains the peptidyl transferase center. Upon binding of either E. coli or Thermus thermophilus RRF to the E. coli ribosome, the tip of ribosomal RNA helix 69 in the large subunit moves away from the small subunit toward RRF by 8 A, thereby disrupting a key contact between the small and large ribosomal subunits termed bridge B2a. In the ribosome crystals, the ability of RRF to destabilize bridge B2a is influenced by crystal packing forces. Movement of helix 69 involves an ordered-to-disordered transition upon binding of RRF to the ribosome. The disruption of bridge B2a upon RRF binding to the ribosome seen in the present structures reveals one of the key roles that RRF plays in ribosome recycling, the dissociation of 70S ribosomes into subunits. The structures also reveal contacts between domain II of RRF and protein S12 in the 30S subunit that may also play a role in ribosome recycling.

Indexed as

Bacterial ProteinsCrystallography, X-RayEscherichia coliEscherichia coli ProteinsModels, MolecularNucleic Acid ConformationProtein BindingProtein Structure, TertiaryRibosomal ProteinsRibosomesRNA, RibosomalThermus thermophilusBacterial ProteinsEscherichia coli ProteinsRibosomal Proteinsribosomal protein S12ribosome releasing factorRNA, Ribosomal

Identifiers

PMID18234219
PMCPMC2712656
OpenAlexW2010257676

What OpenQuestion holds

Textmetadata
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.