Evidence map›Paper›PMID 19759825›Full record

ArticlePloS one2009

The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion.

Patrick Sénéchal, Geneviève Arseneault, Alexandre Leroux, Susan Lindquist, Luis A Rokeach

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

18 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Curing of [PSIPrion · 2018
    Article
  5. Article
  6. Heat shock protein 104 (Hsp104)-mediated curing of [The Journal of biological chemistry · 2017
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Prions in yeast.Genetics · 2012
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. 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

5 authors at 2 institutions in 2 countries.

Patrick SénéchalDepartment of Biochemistry, Université de Montréal, Montréal, Québec, Canada.
Geneviève Arseneault
Alexandre Leroux
Susan Lindquist
Luis A Rokeach
Université de Montréal · CAHoward Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The molecular chaperone Hsp104 is a crucial factor in the acquisition of thermotolerance in yeast. Under stress conditions, the disaggregase activity of Hsp104 facilitates the reactivation of misfolded proteins. Hsp104 is also involved in the propagation of fungal prions. For instance, the well-characterized [PSI(+)] prion of Saccharomyces cerevisiae does not propagate in Deltahsp104 cells or in cells overexpressing Hsp104. In this study, we characterized the functional homolog of Hsp104 from Schizosaccharomyces pombe (Sp_Hsp104). As its S. cerevisiae counterpart, Sp_hsp104(+) is heat-inducible and required for thermotolerance in S. pombe. Sp_Hsp104 displays low disaggregase activity and cannot propagate the [PSI(+)] prion in S. cerevisiae. When overexpressed in S. cerevisiae, Sp_Hsp104 confers thermotolerance to Deltahsp104 cells and reactivates heat-aggregated proteins. However, overexpression of Sp_Hsp104 does not propagate nor eliminate [PSI(+)]. Strikingly, [PSI(+)] was cured by overexpression of a chimeric chaperone bearing the C-terminal domain (CTD) of the S. cerevisiae Hsp104 protein. Our study demonstrates that the ability to untangle aggregated proteins is conserved between the S. pombe and S. cerevisiae Hsp104 homologs, and points to a role of the CTD in the propagation of the S. cerevisiae [PSI(+)] prion.

Indexed as

Adenosine TriphosphatasesFungal ProteinsGene Expression Regulation, FungalHeat-Shock ProteinsHot TemperatureModels, BiologicalMolecular ChaperonesOligonucleotide Array Sequence AnalysisOligonucleotidesPeptide Termination FactorsPrionsProteinsProtein Structure, TertiaryRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSchizosaccharomycesAdenosine TriphosphatasesFungal ProteinsHeat-Shock ProteinsHSP104 protein, S pombeMolecular ChaperonesOligonucleotidesPeptide Termination FactorsPrionsProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiae

Identifiers

PMID19759825
PMCPMC2736384
OpenAlexW2073740978

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.