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Originally published In Press as doi:10.1074/jbc.M102910200 on May 11, 2001

J. Biol. Chem., Vol. 276, Issue 27, 25037-25042, July 6, 2001
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Dioxin-inducible Transactivation in a Chromosomal Setting
ANALYSIS OF THE ACIDIC DOMAIN OF THE Ah RECEPTOR*

Letetia C. JonesDagger and James P. Whitlock Jr.§

From the Dagger  Division of Hematology and Oncology, Cedars Sinai Medical Center, UCLA School of Medicine, Los Angeles, California 90048 and the § Department of Molecular Pharmacology, Stanford University School of Medicine, Stanford, California 94305

We analyzed the transactivation function of the acidic segment of the Ah receptor (amino acids 515-583) by reconstituting AhR-defective mouse hepatoma cells with mutants. Our data reveal that both hydrophobic and acidic residues are important for transactivation and that these residues are clustered in two regions of the acidic segment of AhR. Both regions are crucial for function, because disruption of either one substantially impairs transactivation of the chromosomal CYP1A1 target gene. Neither region contains an amino acid motif that resembles those reported for other acidic activation domains. Furthermore, proline substitutions in both regions do not impair transactivation in vivo, a finding that implies that alpha -helix formation is not required for function.

* This work was supported in part by Research Grant CA 53887 from the National Institutes of Health (to J. P. W.) and by Postdoctoral Fellowship PF-99-127-01-CNE from the American Cancer Society (to L. J.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 650-723-8233; Fax: 650-723-2253; E-mail: jpwhit@stanford.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.