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In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition.
Open accessAbstract
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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“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
In the citing paper
“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]
Citations
Cites
Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589
LIGAND: A versatile computerized approach for characterization of ligand-binding systems
Munson, P. J., & Rodbard, D. (1980) · Analytical Biochemistry · doi:10.1016/0003-2697(80)90515-1 · Cited by 8,373
An analysis of 5'-noncoding sequences from 699 vertebrate messenger RNAs
Kozak, M. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.20.8125 · Cited by 5,090
The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins
Landschulz, W. H., Johnson, P. F., & McKnight, S. L. (1988) · Science · doi:10.1126/science.3289117 · Cited by 3,443
Murre, C., Page-McCaw, P., & Baltimore, D. (1989) · Cell · doi:10.1016/0092-8674(89)90682-x · Cited by 2,713
Poland, A., & Knutson, J. C. (1982) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.22.040182.002505 · Cited by 2,515
Max: A Helix-Loop-Helix Zipper Protein That Forms a Sequence-Specific DNA-Binding Complex with Myc
Blackwood, E. M., & Eisenman, R. N. (1991) · Science · doi:10.1126/science.2006410 · Cited by 1,681
The myoD Gene Family: Nodal Point During Specification of the Muscle Cell Lineage
Weintraub, H. M., Davis, R. L., Tapscott, S. J., Thayer, M., Krause, M., Benezra, R., Blackwell, T. K., Turner, D. L., Rupp, R. A. W., Hollenberg, S. M., et al. (1991) · Science · doi:10.1126/science.1846704 · Cited by 1,581
P450 GENES: STRUCTURE, EVOLUTION, AND REGULATION
Nebert, D. W., & Gonzalez, F. J. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.004501 · Cited by 1,580
Poland, A., Glover, E., & Kende, A. S. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33205-2 · Cited by 1,370
Cloning of a Factor Required for Activity of the Ah (Dioxin) Receptor
Hoffman, E. C., Reyes, H., Chu, F., Sander, F. C., Conley, L. H., Brooks, B. A., & Hankinson, O. (1991) · Science · doi:10.1126/science.1852076 · Cited by 958
Cloning of the Ah-receptor cDNA reveals a distinctive ligand-activated transcription factor.
Burbach, K. M., Poland, A., & Bradfield, C. A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.17.8185 · Cited by 831
Self-citationReyes, H., Reisz‐Porszasz, S., & Hankinson, O. (1992) · Science · doi:10.1126/science.256.5060.1193 · Cited by 777
Turner, R., & Tjian, R. (1989) · Science · doi:10.1126/science.2494701 · Cited by 635
PAS is a dimerization domain common to Drosophila Period and several transcription factors
Huang, Z.-S., Edery, I., & Rosbash, M. (1993) · Nature · doi:10.1038/364259a0 · Cited by 550
A vector for expressing GAL4(1–147) fusions tn mammalian cells
Sadowski, I., & Ptashne, M. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.18.7539 · Cited by 546
Association of the Ah receptor with the 90-kDa heat shock protein.
Perdew, G. H. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68314-0 · Cited by 517
Nambu, J. R., Lewis, J. O., Wharton, K. A., & Crews, S. T. (1991) · Cell · doi:10.1016/0092-8674(91)90292-7 · Cited by 493
cDNA cloning and structure of mouse putative Ah receptor
Ema, M., Sogawa, K., Watanabe, N., Chujoh, Y., Matsushita, N., Gotoh, O., Funae, Y., & Fujii-Kuriyama, Y. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91185-s · Cited by 395
2,3,7,8,-Tetrachlorodibenzo-p-dioxin: segregation of toxocity with the Ah locus.
Poland, A., & Glover, E. A. (1980) · PubMed · Cited by 393
Signal Transduction and Transcriptional Regulation by Glucocorticoid Receptor-LexA Fusion Proteins
Godowski, P. J., Picard, D., & Yamamoto, K. R. (1988) · Science · doi:10.1126/science.3043662 · Cited by 253
Genetic Regulation of Aryl Hydrocarbon Hydroxylase Induction
GIELEN, J. E., Goujon, F. M., & Nebert, D. W. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45624-x · Cited by 248
Pongratz, I., MASON, G. G. F., & Poellinger, L. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42274-0 · Cited by 246
Protein-DNA Interactions at Recognition Sites for the Dioxin-Ah Receptor Complex
Denison, M. S., Fisher, J. M., & Whitlock, J. P. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84730-0 · Cited by 216
Whitelaw, M. L., Pongratz, I., Wilhelmsson, A., Gustafsson, J.-Å., & Poellinger, L. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.4.2504 · Cited by 191
Doren, K. V., Hanahan, D., & Gluzman, Y. (1984) · Journal of Virology · doi:10.1128/jvi.50.2.606-614.1984 · Cited by 170
Dalman, F. C., Bresnick, E. H., Patel, P. D., Perdew, G. H., Watson, S. J., & Pratt, W. B. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47184-6 · Cited by 137
Neuhold, L. A., Shirayoshi, Y., Ozato, K., Jones, J. E., & Nebert, D. W. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.6.2378-2386.1989 · Cited by 135
Photoaffinity labeling of the Ah receptor.
Poland, A., Glover, E. A., Ebetino, F. H., & Kende, A. S. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84570-2 · Cited by 133
Telakowski-Hopkins, C. A., King, R. G., & Pickett, C. B. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.4.1000 · Cited by 118
Elferink, C. J., Gasiewicz, T. A., & Whitlock, J. P. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30561-6 · Cited by 108
Bradfield, C. A., Kende, A. S., & Poland, A. (1988) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)09356-3 · Cited by 95
Self-citationPoland, A., Glover, E., & Bradfield, C. A. (1991) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10876-6 · Cited by 76
Self-citationTranslation of Glucocorticoid Receptor mRNA in Vitro Yields a Nonactivated Protein
Denis, M. G., & Gustafsson, J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83301-4 · Cited by 66
Denison, M. S., & Yao, E. F. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90278-q · Cited by 61
Whitelaw, M. L., Pongratz, I., Wilhelmsson, A., et al. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.4.2504-2514.1993 · Cited by 39
2,3,7,8‐Tetrachlorodibenzo‐p‐dioxin receptors regulate transcription of the cytochrome P1‐450 gene
Durrin, L. K., Jones, P. B. C., Fisher, J. M., Galeazzi, D. R., & Whitlock, J. P. (1987) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240350208 · Cited by 36
Flagged first, then by citations
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Sorted by citations
Wang, G. L., Jiang, B. H., Rue, E. A., & Semenza, G. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5510 · Cited by 6,212
Activation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1
Forsythe, J. A., Jiang, B.-H., Iyer, N. V., Agani, F., Leung, S. W., Koos, R. D., & Semenza, G. L. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.9.4604 · Cited by 3,981
Hayes, J. D., & Pulford, D. J. (1995) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239509083491 · Cited by 3,464
Cellular and developmental control of O 2 homeostasis by hypoxia-inducible factor 1α
Iyer, N. V., Kotch, L. E., Agani, F., Leung, S. W., Laughner, E., Wenger, R. H., Gassmann, M., Gearhart, J. D., Lawler, A. M., Yu, A. Y., et al. (1998) · Genes & Development · doi:10.1101/gad.12.2.149 · Cited by 2,476
INDUCTION OF CYTOCHROME P4501A1
Whitlock, J. P. (1999) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.39.1.103 · Cited by 1,136
Metadata
- Authors
- Dolwick, K. M., Swanson, H. I., & Bradfield, C. A.
- Affiliations
- Northwestern University (US)
- 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
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › 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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