Evidence map›Paper›PMID 25355516›Full record

ArticleNucleic acids research2014

ArfA recognizes the lack of mRNA in the mRNA channel after RF2 binding for ribosome rescue.

Daisuke Kurita, Yuhei Chadani, Akira Muto, Tatsuhiko Abo, Hyouta Himeno

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. 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
2.1field-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

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. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Ribosome Rescue Pathways in Bacteria.Frontiers in microbiology · 2021
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Ribosome pausing, arrest and rescue in bacteria and eukaryotes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  16. Article
  17. 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

5 authors at 2 institutions in 1 country.

Daisuke KuritaDepartment of Biochemistry and Molecular Biology, Faculty of Agriculture and Life Science, Hirosaki University, Hirosaki 036-8561, Japan himeno@cc.hirosaki-u.ac.jp.
Yuhei ChadaniGraduate School of Natural Science and Technology, Okayama University, Okayama 700-8530, Japan.
Akira MutoDepartment of Biochemistry and Molecular Biology, Faculty of Agriculture and Life Science, Hirosaki University, Hirosaki 036-8561, Japan.
Tatsuhiko AboGraduate School of Natural Science and Technology, Okayama University, Okayama 700-8530, Japan Department of Biology, Faculty of Science, Okayama University, Okayama 700-8530, Japan.
Hyouta HimenoDepartment of Biochemistry and Molecular Biology, Faculty of Agriculture and Life Science, Hirosaki University, Hirosaki 036-8561, Japan himeno@cc.hirosaki-u.ac.jp.
Hirosaki University · JPOkayama University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although trans-translation mediated by tmRNA-SmpB has long been known as the sole system to relieve bacterial stalled ribosomes, ArfA has recently been identified as an alternative factor for ribosome rescue in Escherichia coli. This process requires hydrolysis of nascent peptidyl-tRNA by RF2, which usually acts as a stop codon-specific peptide release factor. It poses a fascinating question of how ArfA and RF2 recognize and rescue the stalled ribosome. Here, we mapped the location of ArfA in the stalled ribosome by directed hydroxyl radical probing. It revealed an ArfA-binding site around the neck region of the 30S subunit in which the N- and C-terminal regions of ArfA are close to the decoding center and the mRNA entry channel, respectively. ArfA and RF2 sequentially enter the ribosome stalled in either the middle or 3' end of mRNA, whereas RF2 induces a productive conformational change of ArfA only when ribosome is stalled at the 3' end of mRNA. On the basis of these results, we propose that ArfA functions as the sensor to recognize the target ribosome after RF2 binding.

Indexed as

Binding SitesCysteineEscherichia coli ProteinsModels, MolecularMutationPeptide Termination FactorsProtein BindingRibosomesRNA-Binding ProteinsRNA, MessengerArfA protein, E coliCysteineEscherichia coli ProteinsPeptide Termination FactorsprfB protein, E coliRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID25355516
PMCPMC4245945
OpenAlexW2104164844

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.