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Dioxin-dependent, DNA sequence-specific binding of a multiprotein complex containing the Ah receptor
1Department of Molecular Pharmacology, Stanford University School of Medicine, CA 94305-8233.
Receptor
|January 1, 1994
Summary
Researchers purified the aromatic hydrocarbon (Ah) receptor using DNA affinity chromatography. This revealed the Ah receptor and its binding partner, Arnt, are part of a multiprotein complex involved in dioxin-dependent gene regulation.
Area of Science:
- Molecular biology
- Biochemistry
- Toxicology
Background:
- The aromatic hydrocarbon (Ah) receptor mediates cellular responses to environmental toxins like dioxins.
- Understanding the Ah receptor's structure and function is crucial for toxicology and drug development.
Purpose of the Study:
- To purify and characterize the components of the liganded Ah receptor complex.
- To identify the protein subunits interacting with the Ah receptor's DNA recognition sequence.
Main Methods:
- Affinity chromatography using the Ah receptor's DNA recognition sequence.
- Protein fractionation and molecular weight determination (kDa).
- Immunological assays and cDNA cloning.
Main Results:
- Purified proteins of 110, 106, 98/96, 57, and 54 kDa were identified.
- The 98/96 kDa protein was identified as the Ah receptor nuclear translocator (Arnt).
- The 106 kDa protein was identified as the rat Ah receptor, showing sequence homology with mouse and human counterparts.
Conclusions:
- The Ah receptor and Arnt form a multiprotein complex that binds DNA in a sequence-specific manner.
- DNA recognition site chromatography is an effective method for purifying the Ah receptor.
- Conservation of the N-terminal region suggests functional importance in receptor activity.