Evidence map›Paper›PMID 38661232›Full record

ArticleNucleic acids research2024

The ABCF proteins in Escherichia coli individually cope with 'hard-to-translate' nascent peptide sequences.

Yuhei Chadani, Shun Yamanouchi, Eri Uemura, Kohei Yamasaki, Tatsuya Niwa, Toma Ikeda, Miku Kurihara, Wataru Iwasaki, Hideki Taguchi

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

27 citing papers in PubMed, 27 citations in OpenAlex.

  1. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  2. Collided ribosomes are rescued by the endonuclease Rae1 andbioRxiv : the preprint server for biology · 2026
    Article
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  14. Structural Basis of TACO1-Mediated Efficient Mitochondrial Translation.bioRxiv : the preprint server for biology · 2025
    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

9 authors at 4 institutions in 1 country.

Yuhei ChadaniFaculty of Environmental, Life, Natural Science and Technology, Okayama University, Okayama 700-8530, Japan.ORCID 0000-0003-0862-6676
Shun YamanouchiDepartment of Biological Sciences, Graduate School of Science, the University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.
Eri UemuraCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8503, Japan.
Kohei YamasakiFaculty of Science, Okayama University, Okayama 700-8530, Japan.
Tatsuya NiwaCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8503, Japan.
Toma IkedaSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8503, Japan.
Miku KuriharaSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8503, Japan.
Wataru IwasakiDepartment of Biological Sciences, Graduate School of Science, the University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.ORCID 0000-0002-9169-9245
Hideki TaguchiCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8503, Japan.ORCID 0000-0002-6612-9339
Tokyo Institute of Technology · JPThe University of Tokyo · JPOkayama University · JPOkayama University of Science · JP

Funding

Japan Foundation for Applied EnzymologyJST CREST JPMJCR19S2JST SPRING JPMJSP2108MEXT JP20H05925Ohsumi Frontier Science FoundationTakeda Science FoundationYamada Science Foundation
6 · The paper itself

Abstract

Organisms possess a wide variety of proteins with diverse amino acid sequences, and their synthesis relies on the ribosome. Empirical observations have led to the misconception that ribosomes are robust protein factories, but in reality, they have several weaknesses. For instance, ribosomes stall during the translation of the proline-rich sequences, but the elongation factor EF-P assists in synthesizing proteins containing the poly-proline sequences. Thus, living organisms have evolved to expand the translation capability of ribosomes through the acquisition of translation elongation factors. In this study, we have revealed that Escherichia coli ATP-Binding Cassette family-F (ABCF) proteins, YheS, YbiT, EttA and Uup, individually cope with various problematic nascent peptide sequences within the exit tunnel. The correspondence between noncanonical translations and ABCFs was YheS for the translational arrest by nascent SecM, YbiT for poly-basic sequence-dependent stalling and poly-acidic sequence-dependent intrinsic ribosome destabilization (IRD), EttA for IRD at the early stage of elongation, and Uup for poly-proline-dependent stalling. Our results suggest that ATP hydrolysis-coupled structural rearrangement and the interdomain linker sequence are pivotal for handling 'hard-to-translate' nascent peptides. Our study highlights a new aspect of ABCF proteins to reduce the potential risks that are encoded within the nascent peptide sequences.

Indexed as

ATP-Binding Cassette TransportersEscherichia coliEscherichia coli ProteinsPeptidesAmino Acid SequencePeptide Elongation FactorsProtein BiosynthesisRibosomesATP-Binding Cassette TransportersEscherichia coli Proteinsfactor EF-PPeptide Elongation FactorsPeptides

Identifiers

PMID38661232
PMCPMC11162784
OpenAlexW4395464470

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.