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

DOI Web Site 被引用文献20件
  • Emily C. Hoffman
    Department of Pathology and Laboratory of Biomedical and Environmental Sciences, University of California, Los Angeles, CA 90024
  • Herminio Reyes
    Department of Pathology and Laboratory of Biomedical and Environmental Sciences, University of California, Los Angeles, CA 90024
  • Fong-Fong Chu
    Department of Pathology and Laboratory of Biomedical and Environmental Sciences, University of California, Los Angeles, CA 90024
  • Fred Sander
    Department of Pathology and Laboratory of Biomedical and Environmental Sciences, University of California, Los Angeles, CA 90024
  • Linda H. Conley
    Department of Pathology and Laboratory of Biomedical and Environmental Sciences, University of California, Los Angeles, CA 90024
  • Barbara A. Brooks
    Department of Pathology and Laboratory of Biomedical and Environmental Sciences, University of California, Los Angeles, CA 90024
  • Oliver Hankinson
    Department of Pathology and Laboratory of Biomedical and Environmental Sciences, University of California, Los Angeles, CA 90024

書誌事項

公開日
1991-05-17
DOI
  • 10.1126/science.1852076
公開者
American Association for the Advancement of Science (AAAS)

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説明

<jats:p> 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 <jats:italic>Drosophila</jats:italic> 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. </jats:p>

収録刊行物

  • Science

    Science 252 (5008), 954-958, 1991-05-17

    American Association for the Advancement of Science (AAAS)

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