Evidence map›Paper›PMID 22162769›Full record

ArticlePloS one2011

Nascentome analysis uncovers futile protein synthesis in Escherichia coli.

Koreaki Ito, Yuhei Chadani, Kenta Nakamori, Shinobu Chiba, Yoshinori Akiyama, Tatsuhiko Abo

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

37 citing papers in PubMed, 71 citations in OpenAlex.

  1. Collided ribosomes are rescued by the endonuclease Rae1 andbioRxiv : the preprint server for biology · 2026
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  2. AJournal of bacteriology · 2025
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  9. Sequential rescue and repair of stalled and damaged ribosome by bacterial PrfH and RtcB.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Review
  11. Article
  12. Ribosome Rescue Pathways in Bacteria.Frontiers in microbiology · 2021
    Review
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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

6 authors at 3 institutions in 1 country.

Koreaki ItoFaculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan. kito@cc.kyoto-su.ac.jp
Yuhei Chadani
Kenta Nakamori
Shinobu Chiba
Yoshinori Akiyama
Tatsuhiko Abo
Kyoto Sangyo University · JPOkayama University · JPKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although co-translational biological processes attract much attention, no general and easy method has been available to detect cellular nascent polypeptide chains, which we propose to call collectively a "nascentome." We developed a method to selectively detect polypeptide portions of cellular polypeptidyl-tRNAs and used it to study the generality of the quality control reactions that rescue dead-end translation complexes. To detect nascent polypeptides, having their growing ends covalently attached to a tRNA, cellular extracts are separated by SDS-PAGE in two dimensions, first with the peptidyl-tRNA ester bonds preserved and subsequently after their in-gel cleavage. Pulse-labeled nascent polypeptides of Escherichia coli form a characteristic line below the main diagonal line, because each of them had contained a tRNA of nearly uniform size in the first-dimension electrophoresis but not in the second-dimension. The detection of nascent polypeptides, separately from any translation-completed polypeptides or degradation products thereof, allows us to follow their fates to gain deeper insights into protein biogenesis and quality control pathways. It was revealed that polypeptidyl-tRNAs were significantly stabilized in E. coli upon dysfunction of the tmRNA-ArfA ribosome-rescuing system, whose function had only been studied previously using model constructs. Our results suggest that E. coli cells are intrinsically producing aberrant translation products, which are normally eliminated by the ribosome-rescuing mechanisms.

Indexed as

Bacterial Outer Membrane ProteinsBiochemistryElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelEscherichia coliHydrogen-Ion ConcentrationModels, BiologicalMutationPeptidesPromoter Regions, GeneticProtein BiosynthesisProteomicsRibosomesRNA, TransferRNA, Transfer, Amino AcylTime FactorsBacterial Outer Membrane ProteinsOMPA outer membrane proteinsPeptidesRNA, TransferRNA, Transfer, Amino AcyltRNA, peptidyl-

Identifiers

PMID22162769
PMCPMC3230602
OpenAlexW1986069023

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.