Evidence map›Paper›PMID 28910422›Full record

ArticlePloS one2017

A prolonged chronological lifespan is an unexpected benefit of the [PSI+] prion in yeast.

Kai Wang, Ronald Melki, Mehdi Kabani

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed, 1 pooled it
0.7field-weighted citation impact, top 31% 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

9 citing papers in PubMed, 1 synthesis or guideline pooled it, 15 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Quiescence inAnnual review of genetics · 2022
    Review
  4. Article
  5. Article
  6. Extracellular Vesicles and the Propagation of Yeast Prions.Current topics in microbiology and immunology · 2021
    Article
  7. Review
  8. Prion Amyloid Polymorphs - The Tag Might Change It All.Frontiers in molecular biosciences · 2020
    Article
  9. 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

3 authors at 1 institution in 1 country.

Kai WangParis-Saclay Institute of Neuroscience, Centre National de la Recherche Scientifique, Université Paris-Saclay, Gif-sur-Yvette, France.
Ronald MelkiParis-Saclay Institute of Neuroscience, Centre National de la Recherche Scientifique, Université Paris-Saclay, Gif-sur-Yvette, France.
Mehdi KabaniParis-Saclay Institute of Neuroscience, Centre National de la Recherche Scientifique, Université Paris-Saclay, Gif-sur-Yvette, France.ORCID http://orcid.org/0000-0001-7440-6394
Université Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Self-replicating 'proteinaceous infectious particles' or prions are responsible for complex heritable traits in the yeast Saccharomyces cerevisiae. Our current understanding of the biology of yeast prions stems from studies mostly done in the context of actively dividing cells in optimal laboratory growth conditions. Evidence suggest that fungal prions exist in the wild where most cells are in a non-dividing quiescent state, because of imperfect growth conditions, scarcity of nutrients and competition. We know little about the faithful transmission of yeast prions in such conditions and their physiological consequences throughout the lifespan of yeast cells. We addressed this issue for the [PSI+] prion that results from the self-assembly of the translation release factor Sup35p into insoluble fibrillar aggregates. [PSI+] leads to increased nonsense suppression and confers phenotypic plasticity in response to environmental fluctuations. Here, we report that while [PSI+] had little to no effect on growth per se, it dramatically improved the survival of yeast cells in stationary phase. Remarkably, prolonged chronological lifespan persisted even after [PSI+] was cured from the cells, suggesting that prions may facilitate the acquisition of complex new traits. Such an important selective advantage may contribute to the evolutionary conservation of the prion-forming ability of Sup35p orthologues in distantly related yeast species.

Indexed as

Adaptation, PhysiologicalCell DivisionCell PlasticityPeptide Termination FactorsPhenotypePrionsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsPeptide Termination FactorsPrionsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiae

Identifiers

PMID28910422
PMCPMC5599042
OpenAlexW2754353766

What OpenQuestion holds

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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.