Cloning of a Factor Required for Activity of the Ah (Dioxin) Receptor

The aryl hydrocarbon (Ah) receptor binds various environmental pollutants, such as polycyclic aromatic hydrocarbons, heterocyclic amines, and polychlorinated aromatic compounds (dioxins, dibenzofurans, and biphenyls), and mediates the carcinogenic effects of these agents. The complementary DNA and p...

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Published inScience (American Association for the Advancement of Science) Vol. 252; no. 5008; pp. 954 - 958
Main Authors Hoffman, Emily C., Reyes, Herminio, Chu, Fong-Fong, Sander, Fred, Conley, Linda H., Brooks, Barbara A., Hankinson, Oliver
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for the Advancement of Science 17.05.1991
American Association for the Advancement of Science
The American Association for the Advancement of Science
Subjects
DNA
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Summary:The aryl hydrocarbon (Ah) receptor binds various environmental pollutants, such as polycyclic aromatic hydrocarbons, heterocyclic amines, and polychlorinated aromatic compounds (dioxins, dibenzofurans, and biphenyls), and mediates the carcinogenic effects of these agents. The complementary DNA and part of the gene for an 87-kilodalton human protein that is necessary for Ah receptor function have been cloned. The protein is not the ligand-binding subunit of the receptor but is a factor that is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after binding ligand. The requirement for this factor distinguishes the Ah receptor from the glucocorticoid receptor, to which the Ah receptor has been presumed to be similar. Two portions of the 87-kilodalton protein share sequence similarities with two Drosophila proteins, Per and Sim. Another segment of the protein shows conformity to the consensus sequence for the basic helix-loop-helix motif found in proteins that bind DNA as homodimers or heterodimers.
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FC03-87ER60615
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1852076