Mapping the 90 kDa heat shock protein binding region of the Ah receptor
Abstract
Expression of a series of Ah receptor (AhR) deletion mutants in an in vitro translation system has been previously used to map several functional domains of the murine AhR (Dolwick et al. (1993) Proc. Natl. Acad. Sci. USA 90, 8566‐8570). In this report, quantitative immunoprecipitation of 90‐kDa heat shock protein (hsp90) from reticulocyte lysate allowed us to measure the level of the AhR and AhR deletion mutants complexed with hsp90. After translation of a series of deletion mutants it was determined that there are two distinct domains important in forming a stable AhR/Hsp90 complex, corresponding to amino acid sequences 1‐166 and 289‐347 of the AhR. Neither ARNT, nor Per were able to stably interact with hsp90. Thus, the AhR appears to be a unique member of the PAS domain family of proteins that binds a known ligand and stably interacts with hsp90.
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The PAS B domain of the AhR is involved in both ligand and hsp90 binding.
“Among the various domains of the AhR that exhibit distinct functional activities (1,13-15), we have primarily focused our attention on that of PAS B, one of the two structural repeats (PAS A and PAS B) within the PAS domain, that is involved in both ligand and hsp90 binding.”
From Structural and Functional Characterization of the Aryl Hydrocarbon Receptor Ligand Binding Domain by Homology Modeling and Mutational Analysis (2007) · cites this paper as [15]
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- Authors
- Perdew, G. H., & Bradfield, C. A.
- Affiliations
- Pennsylvania State University (US)
- Northwestern University (US)
- Corresponding author
- Perdew, Gary H.
- Venue
- IUBMB Life
- Publisher
- Wiley
- Published
- 1996-06
- Volume
- 39
- Issue
- 3
- Pages
- 589-593
- ISSN
- 1521-6543 (ISSN-L)
- 1521-6551
- OpenAlex
- W2089908339
- Cited by
- 63
- References
- 0
- Citations by year
- 2025: 1 · 2023: 3 · 2022: 1 · 2021: 2 · 2020: 3 · 2019: 1 · 2018: 2 · 2017: 2 · 2016: 1 · 2015: 4 · 2014: 2 · 2012: 2
- FWCI
- 1.27
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- IUBMB Life (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Environmental Health Sciences (ES04869, ES-05703)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Toxic Organic Pollutants Impact
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Keywords
- aryl hydrocarbon receptor, HSP90, protein-protein interaction, binding domain mapping, deletion mutants, ARNT, PER, ligand binding
- MeSH terms
- Animals, Antibodies, Monoclonal, Binding Sites, DNA-Binding Proteins, Electrophoresis, Polyacrylamide Gel, Mutation, Precipitin Tests, Protein Binding, Transcription Factors, Transcription, Genetic, Protein Biosynthesis, Sequence Deletion, Helix-Loop-Helix Motifs, Receptors, Aryl Hydrocarbon, HSP90 Heat-Shock Proteins, Mice, Aryl Hydrocarbon Receptor Nuclear Translocator
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