Evidence map›Paper›PMID 24652291›Full record

ArticleThe Journal of biological chemistry2014

Ribosomes in a stacked array: elucidation of the step in translation elongation at which they are stalled during S-adenosyl-L-methionine-induced translation arrest of CGS1 mRNA.

Yui Yamashita, Yoshitomo Kadokura, Naoyuki Sotta, Toru Fujiwara, Ichigaku Takigawa, Akiko Satake, Hitoshi Onouchi, Satoshi Naito

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Translational gene regulation in plants: A green new deal.Wiley interdisciplinary reviews. RNA · 2020
    Review
  5. Article
  6. Article
  7. Article
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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 1 country.

Yui YamashitaFrom the Division of Life Science, Graduate School of Life Science, Hokkaido University, Sapporo 060-8589, Japan.
Yoshitomo Kadokura
Naoyuki Sotta
Toru Fujiwara
Ichigaku Takigawa
Akiko Satake
Hitoshi Onouchi
Satoshi Naito
Hokkaido University · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Expression of CGS1, which codes for an enzyme of methionine biosynthesis, is feedback-regulated by mRNA degradation in response to S-adenosyl-L-methionine (AdoMet). In vitro studies revealed that AdoMet induces translation arrest at Ser-94, upon which several ribosomes stack behind the arrested one, and mRNA degradation occurs at multiple sites that presumably correspond to individual ribosomes in a stacked array. Despite the significant contribution of stacked ribosomes to inducing mRNA degradation, little is known about the ribosomes in the stacked array. Here, we assigned the peptidyl-tRNA species of the stacked second and third ribosomes to their respective codons and showed that they are arranged at nine-codon intervals behind the Ser-94 codon, indicating tight stacking. Puromycin reacts with peptidyl-tRNA in the P-site, releasing the nascent peptide as peptidyl-puromycin. This reaction is used to monitor the activity of the peptidyltransferase center (PTC) in arrested ribosomes. Puromycin reaction of peptidyl-tRNA on the AdoMet-arrested ribosome, which is stalled at the pre-translocation step, was slow. This limited reactivity can be attributed to the peptidyl-tRNA occupying the A-site at this step rather than to suppression of PTC activity. In contrast, puromycin reactions of peptidyl-tRNA with the stacked second and third ribosomes were slow but were not as slow as pre-translocation step ribosomes. We propose that the anticodon end of peptidyl-tRNA resides in the A-site of the stacked ribosomes and that the stacked ribosomes are stalled at an early step of translocation, possibly at the P/E hybrid state.

Indexed as

Peptide Chain Elongation, TranslationalAmino Acid SequenceArabidopsis ProteinsBase SequenceBinding SitesCarbon-Oxygen LyasesElectrophoresis, Polyacrylamide GelKineticsModels, GeneticMolecular Sequence DataMutationPeptidesPuromycinRibosomesRNA, MessengerRNA, PlantArabidopsis ProteinsCarbon-Oxygen LyasesO-succinylhomoserine (thiol)-lyasePeptidespeptidyl-puromycinPuromycinRNA, MessengerRNA, PlantRNA, Transfer, Amino AcylS-AdenosylmethioninetRNA, peptidyl-MRNA decaypeptidyl-tRNApuromycin reactionRibosome functionRibosomesribosome stackingTranslationtranslation arrestTranslation regulation

Identifiers

PMID24652291
PMCPMC4007459
OpenAlexW1992282744

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.