Evidence map›Paper›PMID 9632792›Full record

ArticleMolecular and cellular biology1998

Role of the PAS domain in regulation of dimerization and DNA binding specificity of the dioxin receptor.

I Pongratz, C Antonsson, M L Whitelaw, L Poellinger

Abstract read
In one paragraph

Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.5field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

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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

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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

44 citing papers in PubMed, 117 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

I PongratzDepartment of Cell and Molecular Biology, Karolinska Institutet, S-171-77 Stockholm, Sweden.
C Antonsson
M L Whitelaw
L Poellinger
Karolinska Institutet · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The dioxin receptor is a ligand-regulated transcription factor that mediates signal transduction by dioxin and related environmental pollutants. The receptor belongs to the basic helix-loop-helix (bHLH)-Per-Arnt-Sim (PAS) family of factors, which, in addition to the bHLH motif, contain a PAS region of homology. Upon activation, the dioxin receptor dimerizes with the bHLH-PAS factor Arnt, enabling the receptor to recognize xenobiotic response elements in the vicinity of target genes. We have studied the role of the PAS domain in dimerization and DNA binding specificity of the dioxin receptor and Arnt by monitoring the abilities of the individual bHLH domains and different bHLH-PAS fragments to dimerize and bind DNA in vitro and recognize target genes in vivo. The minimal bHLH domain of the dioxin receptor formed homodimeric complexes, heterodimerized with full-length Arnt, and together with Arnt was sufficient for recognition of target DNA in vitro and in vivo. In a similar fashion, only the bHLH domain of Arnt was necessary for DNA binding specificity in the presence of the dioxin receptor bHLH domain. Moreover, the bHLH domain of the dioxin receptor displayed a broad dimerization potential, as manifested by complex formation with, e.g. , the unrelated bHLH-Zip transcription factor USF. In contrast, a construct spanning the dioxin receptor bHLH domain and an N-terminal portion of the PAS domain failed to form homodimers and was capable of dimerizing only with Arnt. Thus, the PAS domain is essential to confer dimerization specificity of the dioxin receptor.

Indexed as

DNA-Binding ProteinsAnimalsAryl Hydrocarbon Receptor Nuclear TranslocatorBasic Helix-Loop-Helix ProteinsCOS CellsDimerizationDNAEndothelial PAS Domain-Containing Protein 1Escherichia coliHelix-Loop-Helix MotifsReceptors, Aryl HydrocarbonRecombinant Fusion ProteinsRegulatory Sequences, Nucleic AcidTrans-ActivatorsTranscription FactorsAryl Hydrocarbon Receptor Nuclear TranslocatorBasic Helix-Loop-Helix ProteinsDNADNA-Binding ProteinsEndothelial PAS Domain-Containing Protein 1Receptors, Aryl HydrocarbonRecombinant Fusion ProteinsTrans-ActivatorsTranscription Factors

Identifiers

PMID9632792
PMCPMC108992
OpenAlexW2139518310

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.