In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition.

Dolwick, K M; Swanson, H I; Bradfield, C A

doi:10.1073/pnas.90.18.8566

Cited by 239Toxic Organic Pollutants ImpactPharmacogenetics and Drug MetabolismNuclear Receptors and Signaling

In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition.

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Dolwick, K M, Swanson, H I, Bradfield, C A·1993·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.90.18.8566PMC PMC47398

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Abstract

The Ah receptor (AHR) is a basic helix-loop-helix protein that mediates the effects of 2,3,7,8-tetrachloro-dibenzo-p-dioxin. In this report, we describe a rabbit reticulocyte system that allows functional expression of both the AHR and its dimeric partner, the AHR nuclear translocator protein (ARNT). By using this in vitro system, we were able to reconstitute agonist binding to the AHR and agonist-induced AHR-ARNT recognition of a cognate DNA enhancer sequence. Expression of AHR deletion mutants revealed the location of N-terminal domains responsible for ligand and DNA recognition and C-terminal domains that play roles in agonist-induced DNA recognition.

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The AhrNG367R mutation lies in the PAS B domain near the predicted ligand and chaperone binding regions.
“Based on previous domain mapping studies, this mutation occurs in the PAS B domain, near a region predicted to encode the ligand and chaperone binding domains (Figure 2, Figure 4) (Dolwick, Swanson, et al., 1993; Fukunaga & Hankinson, 1996).”
From Rodent Genetic Models of Ah Receptor Signaling (2021) · cites this paper as Dolwick, Swanson, et al., 1993
The C-ter loop locates within a previously identified repressor region of approximately 200 residues that could be depressed by agonist-induced receptor transformation.
“Interestingly, this C-ter loop also locates within a previously identified “repressor” region of ~ 200 residues that could be “depressed” by the agonist-induced receptor transformation16.”
From Structural basis for the ligand-dependent activation of heterodimeric AHR-ARNT complex (2025) · cites this paper as [16]

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Self-citation

Authors: Dolwick, K. M., Swanson, H. I., & Bradfield, C. A.
Affiliations: Northwestern University (US)
ORCID: Swanson, H I
Bradfield, C A
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1993-09-15
Volume: 90
Issue: 18
Pages: 8566-8570
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.90.18.8566
PMC: PMC47398
OpenAlex: W1979697640
Cited by: 239
References: 37
Citations by year: 2026: 2 · 2025: 1 · 2023: 4 · 2022: 4 · 2021: 5 · 2020: 4 · 2019: 1 · 2018: 7 · 2017: 6 · 2016: 2 · 2015: 3 · 2014: 6 · 2013: 4 · 2012: 3
FWCI: 17.52
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Cancer Institute (T32 CA09560, T32CA009560)
National Institute of Environmental Health Sciences (ES-05703, F32ES005589, ES-05589)
Topics: Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Toxic Organic Pollutants Impact
Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
Keywords: aryl hydrocarbon receptor, ligand binding, DNA recognition, enhancers, bHLH transcription factors, 2,3,7,8-tetrachlorodibenzo-p-dioxin
MeSH terms: Polychlorinated Dibenzodioxins, Animals, Base Sequence, Binding Sites, Codon, DNA, Ligands, Molecular Sequence Data, Oligodeoxyribonucleotides, Rabbits, Receptors, Drug, Reticulocytes, Transcription, Genetic, Protein Biosynthesis, Blotting, Western, Polymerase Chain Reaction, Mutagenesis, Site-Directed, Sequence Deletion, Receptors, Aryl Hydrocarbon, Mice

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In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition.

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