Evidence map›Paper›PMID 36881630›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

Cooperative action of separate interaction domains promotes high-affinity DNA binding of

Mattia Fontana, Mark Roosjen, Isidro Crespo García, Willy van den Berg, Marc Malfois, Roeland Boer, Dolf Weijers, Johannes Hohlbein

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
8.7field-weighted citation impact, top 3% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Transcription Factors in Plant Gene Expression Regulation.International journal of molecular sciences · 2025
    Article
  7. A conserved ARF-DNA interface underlies auxin-triggered transcriptional response.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. 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

8 authors at 2 institutions in 2 countries.

Mattia FontanaLaboratory of Biophysics, Wageningen University and Research, 6708 WE Wageningen, The Netherlands.ORCID 0000-0003-2640-0451
Mark RoosjenLaboratory of Biochemistry, Wageningen University and Research, 6708 WE Wageningen, The Netherlands.
Isidro Crespo GarcíaALBA synchrotron Light Source, Cerdanyola del Vallès, Barcelona 08290, Spain.ORCID 0000-0001-7698-1720
Willy van den BergLaboratory of Biochemistry, Wageningen University and Research, 6708 WE Wageningen, The Netherlands.ORCID 0000-0002-2882-2351
Marc MalfoisALBA synchrotron Light Source, Cerdanyola del Vallès, Barcelona 08290, Spain.ORCID 0000-0001-5231-1896
Roeland BoerALBA synchrotron Light Source, Cerdanyola del Vallès, Barcelona 08290, Spain.ORCID 0000-0001-5949-6627
Dolf WeijersLaboratory of Biochemistry, Wageningen University and Research, 6708 WE Wageningen, The Netherlands.ORCID 0000-0003-4378-141X
Johannes HohlbeinLaboratory of Biophysics, Wageningen University and Research, 6708 WE Wageningen, The Netherlands.ORCID 0000-0001-7436-2221
Wageningen University & Research · NLALBA Synchrotron (Spain) · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The signaling molecule auxin coordinates many growth and development processes in plants, mainly through modulating gene expression. Transcriptional response is mediated by the family of auxin response factors (ARF). Monomers of this family recognize a DNA motif and can homodimerize through their DNA-binding domain (DBD), enabling cooperative binding to an inverted binding site. Most ARFs further contain a C-terminal PB1 domain that is capable of homotypic interactions and mediating interactions with Aux/IAA repressors. Given the dual role of the PB1 domain, and the ability of both DBD and PB1 domain to mediate dimerization, a key question is how these domains contribute to DNA-binding specificity and affinity. So far, ARF-ARF and ARF-DNA interactions have mostly been approached using qualitative methods that do not provide a quantitative and dynamic view on the binding equilibria. Here, we utilize a DNA binding assay based on single-molecule Förster resonance energy transfer (smFRET) to study the affinity and kinetics of the interaction of several

Indexed as

ArabidopsisArabidopsis ProteinsTranscription FactorsBinding SitesIndoleacetic AcidsArabidopsis ProteinsIndoleacetic AcidsTranscription Factorsauxin response factorfour-state cyclic modelprotein–DNA interactionsmFRETtranscription factor

Identifiers

PMID36881630
PMCPMC10089223
OpenAlexW4323348131

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.