Evidence map›Paper›PMID 8913738›Full record

ArticleGenetics1996

Synergy between trehalose and Hsp104 for thermotolerance in Saccharomyces cerevisiae.

B Elliott, R S Haltiwanger, B Futcher

Abstract read
In one paragraph

Article in Genetics, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
–field-weighted citation impact
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

49 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Compatible solutes determine the heat resistance of conidia.Fungal biology and biotechnology · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The involvement of theVirulence · 2021
    Article
  11. Molecular Mechanisms of Conidial Germination inMicrobiology and molecular biology reviews : MMBR · 2020
    Review
  12. DAF-16/FoxO inCells · 2020
    Review
  13. Article
  14. Article
  15. Article
  16. eLife · 2017
    Article
  17. Review
  18. mBio · 2017
    Article
  19. Review
  20. Review
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.

B ElliottCold Spring Harbor Laboratory, New York 11724, USA.
R S Haltiwanger
B Futcher

Funding

SIZE CONTROL &COMMITMENT TO DIVISION IN S. CEREVISIAER01GM039978 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI FUTCHER, BRUCE BRUCE · 1988 to 2014
$4.3M
WIN CELL CYCLE CLOCKS IN S CEREVISIAER01GM045410 · NIGMS · COLD SPRING HARBOR LABORATORY · PI FUTCHER, ALLEN BRUCE · 1991 to 1999
–
GLYCOSYLATION OF NUCLEAR AND CYTOPLASMIC PROTEINSR01GM048666 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI HALTIWANGER, ROBERT S. · 1993 to 1997
–
NIGMS NIH HHS GM-39978NIGMS NIH HHS GM-45410NIGMS NIH HHS GM-48666
6 · The paper itself

Abstract

We isolated a mutant strain unable to acquire heat shock resistance in stationary phase. Two mutations contributed to this phenotype. One mutation was at the TPS2 locus, which encodes trehalose-6-phosphate phosphatase. The mutant fails to make trehalose and accumulates trehalose-6-phosphate. The other mutation was at the HSP104 locus. Gene disruptions showed that tps2 and hsp104 null mutants each produced moderate heat shock sensitivity in stationary phase cells. The two mutations were synergistic and the double mutant had little or no stationary phase-induced heat shock resistance. The same effect was seen in the tps1 (trehalose-6-phosphate synthase) hsp104 double mutant, suggesting that the extreme heat shock sensitivity was due mainly to a lack of trehalose rather than to the presence of trehalose-6-phosphate. However, accumulation of trehalose-6-phosphate did cause some phenotypes in the tps2 mutant, such as temperature sensitivity for growth. Finally, we isolated a high copy number suppressor of the temperature sensitivity of tps2, which we call PMU1, which reduced the levels of trehalose-6-phosphate in tps2 mutants. The encoded protein has a region homologous to the active site of phosphomutases.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceCloning, MolecularFungal ProteinsHeatingHeat-Shock ProteinsMolecular Sequence DataPhosphoric Monoester HydrolasesSaccharomyces cerevisiaeSuppression, GeneticTrehaloseFungal ProteinsHeat-Shock ProteinsHsP104 protein, S cerevisiaePhosphoric Monoester HydrolasesSaccharomyces cerevisiae ProteinsTrehalosetrehalose-phosphatase

Identifiers

PMID8913738
PMCPMC1207632

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.