Evidence map›Paper›PMID 7761443›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Disruption of the gene for hsp30, an alpha-crystallin-related heat shock protein of Neurospora crassa, causes defects in thermotolerance.

N Plesofsky-Vig, R Brambl

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Differential Roles of Three α-Crystallin Domain-Containing sHsps ofInternational journal of molecular sciences · 2022
    Article
  3. Article
  4. Article
  5. Regulated Forms of Cell Death in Fungi.Frontiers in microbiology · 2017
    Review
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  7. Article
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  10. Review
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  14. Article
  15. Review
  16. Article
  17. Article
  18. Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  19. Article
  20. Small heat shock protein of Methanococcus jannaschii, a hyperthermophile.Proceedings of the National Academy of Sciences of the United States of America · 1998
    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

2 authors at 1 institution in 1 country.

N Plesofsky-VigDepartment of Genetics and Cell Biology, University of Minnesota, St. Paul 55108, USA.
R Brambl
University of Minnesota · US

Funding

MOLECULAR BIOLOGY OF MITOCHONDRIA IN NEUROSPORA CRASSAR01GM019398 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI BRAMBL, ROBERT M · 1985 to 1998
–
NIGMS NIH HHS GM-19398
6 · The paper itself

Abstract

The alpha-crystallin-related heat shock proteins are produced by all eukaryotes, but the role of these proteins in thermoprotection remains unclear. To investigate the function of one of these proteins, we disrupted expression of the single-copy hsp30 gene of Neurospora crassa, using repeat-induced point mutagenesis, and we generated and characterized mutant strains that were deficient in hsp30 synthesis. These strains could grow at high temperature and they acquired thermotolerance from a heat shock. However, the hsp30-defective strains proved to be extremely sensitive to the combined stresses of high temperature and carbohydrate limitation, enforced by the addition of a nonmetabolizable glucose analogue. Under these conditions, their survival was reduced by 90% compared with wild-type cells. This sensitive phenotype was reversed by reintroduction of a functional hsp30 gene into the mutant strains. The mutant cells contained mitochondria from which a 22-kDa protein was readily extracted with detergents, in contrast to its retention by the mitochondria of wild-type cells. Antibodies against hsp30 coimmunoprecipitated a protein also of approximately 22 kDa from wild-type cells. Results of this study suggest that hsp30 may be important for efficient carbohydrate utilization during high temperature stress and that it may interact with other mitochondrial membrane proteins and function as a protein chaperone.

Indexed as

Genes, FungalCloning, MolecularCrosses, GeneticDNA, FungalEscherichia coliHeat-Shock ProteinsHot TemperatureHSP30 Heat-Shock ProteinsMembrane ProteinsMitochondriaMutagenesisMutagenesis, Site-DirectedNeurospora crassaPhenotypePlasmidsPoint MutationDNA, FungalHeat-Shock ProteinsHSP30 Heat-Shock ProteinsMembrane ProteinsRecombinant Fusion Proteins

Identifiers

PMID7761443
PMCPMC41842
OpenAlexW2004684296

What OpenQuestion holds

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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.