Evidence map›Paper›PMID 20534490›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Ribosome recycling step in yeast cytoplasmic protein synthesis is catalyzed by eEF3 and ATP.

Shinya Kurata, Klaus H Nielsen, Sarah F Mitchell, Jon R Lorsch, Akira Kaji, Hideko Kaji

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

24 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. The geneFrontiers in microbiology · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Transcriptomic analysis ofF1000Research · 2017
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. The ABCs of the ribosome.Nature structural & molecular biology · 2014
    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

6 authors at 4 institutions in 2 countries.

Shinya KurataDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, 1020 Locust Street, Philadelphia, PA 19107, USA.
Klaus H Nielsen
Sarah F Mitchell
Jon R Lorsch
Akira Kaji
Hideko Kaji
Johns Hopkins University · USThomas Jefferson University · USAarhus University · DKUniversity of Pennsylvania · US

Funding

RIBOSOME RECYCLING FACTOR(RRF) IN PROKARYOTESR01GM060429 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI KAJI, AKIRA · 2001 to 2004
$1.1M
NIGMS NIH HHS GM60429NIGMS NIH HHS R01 GM060429
6 · The paper itself

Abstract

After each round of protein biosynthesis, the posttermination complex (PoTC) consisting of a ribosome, mRNA, and tRNA must be disassembled into its components for a new round of translation. Here, we show that a Saccharomyces cerevisiae model PoTC was disassembled by ATP and eukaryotic elongation factor 3 (eEF3). GTP or ITP functioned with less efficiency and adenosine 5gamma'-(beta,gamma-imido)triphosphate did not function at all. The k(cat) of eEF3 was 1.12 min(-1), which is comparable to that of the in vitro initiation step. The disassembly reaction was inhibited by aminoglycosides and cycloheximide. The subunits formed from the yeast model PoTC remained separated under ionic conditions close to those existing in vivo, suggesting that they are ready to enter the initiation process. Based on our experimental techniques used in this paper, the release of mRNA and tRNA and ribosome dissociation took place simultaneously. No 40S*mRNA complex was observed, indicating that eEF3 action promotes ribosome recycling, not reinitiation.

Indexed as

Adenosine TriphosphateCytoplasmKineticsModels, BiologicalModels, MolecularPeptide Elongation FactorsRibosomesRNA, FungalRNA, MessengerRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatePeptide Elongation FactorsRNA, FungalRNA, MessengerRNA, TransferSaccharomyces cerevisiae Proteins

Identifiers

PMID20534490
PMCPMC2890720
OpenAlexW2003084616

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.