Evidence map›Paper›PMID 24874105›Full record

ArticlePloS one2014

Interaction studies of the human and Arabidopsis thaliana Med25-ACID proteins with the herpes simplex virus VP16- and plant-specific Dreb2a transcription factors.

Ximena Aguilar, Jeanette Blomberg, Kristoffer Brännström, Anders Olofsson, Jürgen Schleucher, Stefan Björklund

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. The potent PHL4 transcription factor effector domain contains significant disorder.Protein science : a publication of the Protein Society · 2024
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  7. Suppression ofFrontiers in plant science · 2020
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. The Multitalented MEDIATOR25.Frontiers in plant science · 2017
    Review
  13. Article
  14. Review
  15. 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

6 authors at 1 institution in 1 country.

Ximena AguilarDepartment of Chemistry, Umeå University, Umeå, Sweden.
Jeanette BlombergDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Kristoffer BrännströmDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Anders OlofssonDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Jürgen SchleucherDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Stefan BjörklundDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Umeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mediator is an evolutionary conserved multi-protein complex present in all eukaryotes. It functions as a transcriptional co-regulator by conveying signals from activators and repressors to the RNA polymerase II transcription machinery. The Arabidopsis thaliana Med25 (aMed25) ACtivation Interaction Domain (ACID) interacts with the Dreb2a activator which is involved in plant stress response pathways, while Human Med25-ACID (hMed25) interacts with the herpes simplex virus VP16 activator. Despite low sequence similarity, hMed25-ACID also interacts with the plant-specific Dreb2a transcriptional activator protein. We have used GST pull-down-, surface plasmon resonance-, isothermal titration calorimetry and NMR chemical shift experiments to characterize interactions between Dreb2a and VP16, with the hMed25 and aMed25-ACIDs. We found that VP16 interacts with aMed25-ACID with similar affinity as with hMed25-ACID and that the binding surface on aMed25-ACID overlaps with the binding site for Dreb2a. We also show that the Dreb2a interaction region in hMed25-ACID overlaps with the earlier reported VP16 binding site. In addition, we show that hMed25-ACID/Dreb2a and aMed25-ACID/Dreb2a display similar binding affinities but different binding energetics. Our results therefore indicate that interaction between transcriptional regulators and their target proteins in Mediator are less dependent on the primary sequences in the interaction domains but that these domains fold into similar structures upon interaction.

Indexed as

Protein Interaction Domains and MotifsArabidopsisArabidopsis ProteinsDNA-Binding ProteinsHerpes Simplex Virus Protein Vmw65HumansKineticsMediator ComplexModels, MolecularMultiprotein ComplexesNuclear Magnetic Resonance, BiomolecularNuclear ProteinsProtein BindingProtein ConformationThermodynamicsTranscription FactorsArabidopsis ProteinsDNA-Binding ProteinsDREB2A protein, ArabidopsisHerpes Simplex Virus Protein Vmw65MED25 protein, humanMediator ComplexMultiprotein ComplexesNuclear ProteinsPFT1 protein, ArabidopsisTranscription Factors

Identifiers

PMID24874105
PMCPMC4038590
OpenAlexW2125290101

What OpenQuestion holds

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LicenceCC BY
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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.