Evidence map›Paper›PMID 25154418›Full record

ArticleMolecular and cellular biology2014

Release factor eRF3 mediates premature translation termination on polylysine-stalled ribosomes in Saccharomyces cerevisiae.

Marco Chiabudini, Arlette Tais, Ying Zhang, Sachiko Hayashi, Tina Wölfle, Edith Fitzke, Sabine Rospert

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2014. 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
2.6field-weighted citation impact, top 10% 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, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Ribosome Molecular Aging Shapes Translation Dynamics.bioRxiv : the preprint server for biology · 2026
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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

7 authors at 1 institution in 1 country.

Marco ChiabudiniInstitute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg, Freiburg, Germany Center for Biological Signaling Studies (BIOSS), University of Freiburg, Freiburg, Germany.
Arlette TaisInstitute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg, Freiburg, Germany.
Ying ZhangInstitute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg, Freiburg, Germany.
Sachiko HayashiInstitute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg, Freiburg, Germany.
Tina WölfleInstitute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg, Freiburg, Germany.
Edith FitzkeInstitute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg, Freiburg, Germany.
Sabine RospertInstitute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg, Freiburg, Germany Center for Biological Signaling Studies (BIOSS), University of Freiburg, Freiburg, Germany sabine.rospert@biochemie.uni-freiburg.de.
University of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosome stalling is an important incident enabling the cellular quality control machinery to detect aberrant mRNA. Saccharomyces cerevisiae Hbs1-Dom34 and Ski7 are homologs of the canonical release factor eRF3-eRF1, which recognize stalled ribosomes, promote ribosome release, and induce the decay of aberrant mRNA. Polyadenylated nonstop mRNA encodes aberrant proteins containing C-terminal polylysine segments which cause ribosome stalling due to electrostatic interaction with the ribosomal exit tunnel. Here we describe a novel mechanism, termed premature translation termination, which releases C-terminally truncated translation products from ribosomes stalled on polylysine segments. Premature termination during polylysine synthesis was abolished when ribosome stalling was prevented due to the absence of the ribosomal protein Asc1. In contrast, premature termination was enhanced, when the general rate of translation elongation was lowered. The unconventional termination event was independent of Hbs1-Dom34 and Ski7, but it was dependent on eRF3. Moreover, premature termination during polylysine synthesis was strongly increased in the absence of the ribosome-bound chaperones ribosome-associated complex (RAC) and Ssb (Ssb1 and Ssb2). On the basis of the data, we suggest a model in which eRF3-eRF1 can catalyze the release of nascent polypeptides even though the ribosomal A-site contains a sense codon when the rate of translation is abnormally low.

Indexed as

Adaptor Proteins, Signal TransducingAdenosine TriphosphatasesCodon, TerminatorGTP-Binding ProteinsHSP70 Heat-Shock ProteinsPeptide Termination FactorsPolylysineProtein Processing, Post-TranslationalRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesASC1 protein, S cerevisiaeCodon, TerminatorGTP-Binding ProteinsHSP70 Heat-Shock Proteinspeptide-chain-release factor 3Peptide Termination FactorsPolylysineSaccharomyces cerevisiae ProteinsSSB1 protein, S cerevisiaeSSB2 protein, S cerevisiaeSUP35 protein, S cerevisiaeSUP45 protein, S cerevisiae

Identifiers

PMID25154418
PMCPMC4386461
OpenAlexW2128406191

What OpenQuestion holds

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Registered trials

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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.