Evidence map›Paper›PMID 19015537›Full record

ArticleGenetics2009

Curing of yeast [URE3] prion by the Hsp40 cochaperone Ydj1p is mediated by Hsp70.

Deepak Sharma, Robert F Stanley, Daniel C Masison

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

28 citing papers in PubMed, 37 citations in OpenAlex.

  1. Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025
    Review
  2. Article
  3. Human proteins curing yeast prions.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Review
  5. Differential Interactions of Molecular Chaperones and Yeast Prions.Journal of fungi (Basel, Switzerland) · 2022
    Review
  6. Mechanisms for Curing Yeast Prions.International journal of molecular sciences · 2020
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Prions, Chaperones, and Proteostasis in Yeast.Cold Spring Harbor perspectives in biology · 2017
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013
    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 2 institutions in 1 country.

Deepak SharmaLaboratory of Biochemistry and Genetics, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0851, USA.
Robert F Stanley
Daniel C Masison
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

Yeast prions and Hsp70 co-chaperonesZIADK024952 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI MASISON, DANIEL · 2009 to 2015
$2.1M
Yeast prions and Hsp70 co-chaperonesZ01DK024952 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI MASISON, DANIEL · 2007 to 2008
$493k
Intramural NIH HHS
6 · The paper itself

Abstract

[URE3] is a prion of the yeast Ure2 protein. Hsp40 is a cochaperone that regulates Hsp70 chaperone activity. When overexpressed, the Hsp40 Ydj1p cures yeast of [URE3], but the Hsp40 Sis1p does not. On the basis of biochemical data Ydj1p has been proposed to cure [URE3] by binding soluble Ure2p and preventing it from joining prion aggregates. Here, we mutagenized Ydj1p and find that disrupting substrate binding, dimerization, membrane association, or ability to transfer substrate to Hsp70 had little or no effect on curing. J-domain point mutations that disrupt functional interactions of Ydj1p with Hsp70 abolished curing, and the J domain alone cured [URE3]. Consistent with heterologous J domains possessing similar Hsp70 regulatory activity, the Sis1p J domain also cured [URE3]. We further show that Ydj1p is not essential for [URE3] propagation and that depletion of Ure2p is lethal in cells lacking Ydj1p. Our data imply that curing of [URE3] by overproduced Ydj1p does not involve direct interaction of Ydj1p with Ure2p but rather works through regulation of Hsp70 through a specific J-protein/Hsp70 interaction.

Indexed as

Glutathione PeroxidaseHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMicrobial ViabilityMutant ProteinsMutationPrenylationPrionsProtein MultimerizationProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpores, FungalGlutathione PeroxidaseHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMutant ProteinsPrionsSaccharomyces cerevisiae ProteinsSIS1 protein, S cerevisiaeURE2 protein, S cerevisiaeYDJ1 protein, S cerevisiae

Identifiers

PMID19015537
PMCPMC2621161
OpenAlexW2130210568

What OpenQuestion holds

Textmetadata
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.