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Cited by 91Toxic Organic Pollutants ImpactPharmacogenetics and Drug MetabolismGenomics and Chromatin Dynamics

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Identification of a Novel Domain in the Aryl Hydrocarbon Receptor Required for DNA Binding

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Fukunaga, Bert N., Hankinson, Oliver·1996·Journal of Biological Chemistry
DOI 10.1074/jbc.271.7.3743
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Abstract

The aryl hydrocarbon receptor (AHR) is a ligand-activated transcription factor that binds DNA in the form of a heterodimer with the AHR nuclear translocator protein (ARNT). Both proteins possess basic helix-loop-helix motifs. ARNT binds to the side of the xenobiotic responsive element (XRE) that resembles an E-box (the sequence recognized by the majority of other basic helix-loop-helix proteins), whereas AHR binds to the side of the XRE that does not conform to the E-box sequence. The basic region of ARNT closely resembles those of other E-box-binding proteins, whereas the "nominal basic region" of AHR (amino acids 27 39), although required for XRE binding, deviates from this consensus. By extensive mutational analysis it is shown here that an additional block of amino acids of AHR (from tyrosine 9 to lysine 20) that contains a highly basic segment is required for XRE binding and transcriptional activation. Deletion of the first nine amino acids negates XRE binding. Substitution of either tyrosine 9 or arginine 14 with alanine eliminates XRE binding, whereas alanine substitutions at certain other sites within the block reduce but do not eliminate binding. The reported absence of the first nine amino acids in the purified protein may therefore be artifactual. These results suggest that the amino acids of AHR involved in binding to the XRE constitute a novel DNA-binding domain, comprising amino acids located within and amino-terminal to the nominal basic region.

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Crossref · 10.1074/jbc.271.7.3743

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  • The bHLH domain of AHR is responsible for nuclear localization, DNA binding, and dimerization with ARNT.

    “The bHLH domain has been shown to be responsible for nuclear localization, DNA binding, and dimerization with the obligate partner, the Aryl Hydrocarbon Nuclear Translocator (ARNT) (Burbach et al., 1992; Bert N. Fukunaga & Hankinson, 1996; Sanjay Jain et al., 1994).”

    From Rodent Genetic Models of Ah Receptor Signaling (2021) · cites this paper as Bert N. Fukunaga & Hankinson, 1996

    The paper’s Abstract reports that AHR’s nominal basic region is required for DNA binding, alongside amino acids immediately before it. It also says AHR binds DNA as a heterodimer with ARNT, but attributes a contribution to their dimerization to the PAS domain. The passages do not establish that the bHLH domain is responsible for nuclear localization or for dimerization with ARNT. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • 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 Fukunaga & Hankinson, 1996

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Citations

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Metadata

Authors
Fukunaga, B. N., & Hankinson, O.
Affiliations
University of California, Los Angeles (US)
Corresponding author
Hankinson, Oliver
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1996-02
Volume
271
Issue
7
Pages
3743-3749
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.271.7.3743
OpenAlex
W1980552888
Cited by
91
References
4
Citations by year
2026: 1 · 2025: 2 · 2024: 1 · 2023: 1 · 2021: 1 · 2020: 5 · 2019: 1 · 2018: 2 · 2017: 1 · 2016: 4 · 2015: 2 · 2014: 1 · 2013: 3 · 2012: 2
FWCI
6.50
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
National Cancer Institute (R01CA028868)
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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords
aryl hydrocarbon receptor, DNA-binding domain, xenobiotic response element, ARNT, basic helix-loop-helix proteins, transcriptional activation, ligand-activated transcription factors, E-box
MeSH terms
Alanine, Amino Acid Sequence, Animals, Base Sequence, Binding Sites, DNA, DNA Mutational Analysis, DNA-Binding Proteins, Humans, Ligands, Mammals, Molecular Sequence Data, Recombinant Fusion Proteins, Transcription Factors, Transcription, Genetic, Protein Biosynthesis, Xenobiotics, Polymerase Chain Reaction, Mutagenesis, Site-Directed, Consensus Sequence, Sequence Homology, Amino Acid, DNA Primers, Helix-Loop-Helix Motifs, Receptors, Aryl Hydrocarbon, Macromolecular Substances, Rats, Aryl Hydrocarbon Receptor Nuclear Translocator

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