Evidence map›Paper›PMID 15526206›Full record

ArticleCurrent genetics2004

The gene for the heat-shock protein HSP100 is induced by blue light and heat-shock in the fungus Phycomyces blakesleeanus.

Julio Rodríguez-Romero, Luis M Corrochano

Abstract read
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In one paragraph

Article in Current genetics, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

10 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Light regulation of metabolic pathways in fungi.Applied microbiology and biotechnology · 2010
    Review
  7. Phycomyces MADB interacts with MADA to form the primary photoreceptor complex for fungal phototropism.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  8. Article
  9. Article
  10. The Phycomyces madA gene encodes a blue-light photoreceptor for phototropism and other light responses.Proceedings of the National Academy of Sciences of the United States of America · 2006
    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.

Julio Rodríguez-RomeroDepartamento de Genética, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes 6, Apartado 1095, 41080 Sevilla, Spain.
Luis M Corrochano
Universidad de Sevilla · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We cloned and sequenced the Phycomyces hspA gene. The hspA gene product is a 901-amino-acid protein member of the clpB/HSP100 family. HSP100 proteins are ATPases involved in high-temperature tolerance, proteolysis, and protein disaggregation. Phycomyces HSP100 is composed of a domain presumably involved in protein-protein interactions and two ATP-binding domains. The hspA promoter contains three heat-shock elements that are presumably involved in the activation of hspA after heat-shock. In addition, four short sequences are present in the hspA promoter and in the promoter of the photoinducible genes carB and carRA; and these are candidates as binding sites for light-regulated transcription factors. Blue light can increase transcription of the hspA gene 10-fold, with a threshold of 1 J/m2. The threshold for hspA photoactivation is 10(4) times higher than the thresholds for blue-light regulation of sporangiophore development and photocarotenogenesis, which suggests that there are differences in the photosensory systems for gene photoactivation and mycelial photoresponses. A heat-shock of 30 min at 34 degrees C or 42 degrees C increased hspA gene activity 160-fold. The differences in maximum hspA gene transcription by blue light and heatshock suggest the presence of different regulatory mechanisms.

Indexed as

Hot TemperatureLightTranscription, GeneticAdenosine TriphosphatasesAmino Acid SequenceBacterial ProteinsBase SequenceBinding SitesCarotenoidsCloning, MolecularGene Expression Regulation, FungalHeat-Shock ProteinsHeat-Shock ResponseMolecular Sequence DataPhotochemistryPhycomycesAdenosine TriphosphatasesBacterial ProteinsCarotenoidsHeat-Shock Proteins

Identifiers

PMID15526206
OpenAlexW1988508028

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.