Evidence map›Paper›PMID 15247379›Full record

ArticlePlant physiology2004

Role of Hsp17.4-CII as coregulator and cytoplasmic retention factor of tomato heat stress transcription factor HsfA2.

Markus Port, Joanna Tripp, Dirk Zielinski, Christian Weber, Dirk Heerklotz, Sybille Winkelhaus, Daniela Bublak, Klaus-Dieter Scharf

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

38 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Article
  3. Impact of heat stress on physiological characteristics and expression of heat shock proteins (HSPs) in groundnut (Physiology and molecular biology of plants : an international journal of functional plant biology · 2024
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. An overview of heat stress in tomato (Saudi journal of biological sciences · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

8 authors at 1 institution in 1 country.

Markus PortBiocenter of the Goethe University, D-60439 Frankfurt am Main, Germany.
Joanna Tripp
Dirk Zielinski
Christian Weber
Dirk Heerklotz
Sybille Winkelhaus
Daniela Bublak
Klaus-Dieter Scharf
Goethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HsfA2 is a heat stress (hs)-induced Hsf in peruvian tomato (Lycopersicon peruvianum) and the cultivated form Lycopersicon esculentum. Due to the high activator potential and the continued accumulation during repeated cycles of heat stress and recovery, HsfA2 becomes a dominant Hsf in thermotolerant cells. The formation of heterooligomeric complexes with HsfA1 leads to nuclear retention and enhanced transcriptional activity of HsfA2. This effect seems to represent one part of potential molecular mechanisms involved in its activity control. As shown in this paper, the activity of HsfA2 is also controlled by a network of nucleocytoplasmic small Hsps influencing its solubility, intracellular localization and activator function. By yeast two-hybrid interaction and transient coexpression studies in tobacco (Nicotiana plumbaginifolia) mesophyll protoplasts, we found that tomato (Lycopersicon esculentum) Hsp17.4-CII acts as corepressor of HsfA2. Given appropriate conditions, both proteins together formed large cytosolic aggregates which could be solubilized in presence of class CI sHsps. However, independent of the formation of aggregates or of the nucleocytoplasmic distribution of HsfA2, its transcriptional activity was specifically repressed by interaction of Hsp17.4-CII with the C-terminal activator domain. Although not identical in all aspects, the situation with the highly expressed, heat stress-inducible Arabidopsis HsfA2 was found to be principally similar. In corresponding reporter assays its activity was repressed in presence of AtHsp17.7-CII but not of AtHsp17.6-CII or LpHsp17.4-CII.

Indexed as

Arabidopsis ProteinsBase SequenceCytoplasmDNA-Binding ProteinsDNA PrimersElectrophoresis, Polyacrylamide GelHeat-Shock ProteinsHeat Shock Transcription FactorsHot TemperatureMolecular Sequence DataNicotianaPlant ProteinsProtoplastsSolanum lycopersicumTranscription FactorsArabidopsis ProteinsDNA-Binding ProteinsDNA PrimersHeat-Shock ProteinsHeat Shock Transcription FactorsHSFA2 protein, ArabidopsisPlant ProteinsTranscription Factors

Identifiers

PMID15247379
PMCPMC519062
OpenAlexW2010670457

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.