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J Biol Chem, Vol. 274, Issue 21, 15159-15166, May 21, 1999

Two Forms of Aryl Hydrocarbon Receptor Type 2 in Rainbow Trout (Oncorhynchus mykiss)
EVIDENCE FOR DIFFERENTIAL EXPRESSION AND ENHANCER SPECIFICITY

Christian C. Abnet, Robert L. Tanguay, Mark E. Hahn^§, Warren Heideman, and Richard E. Peterson

From the  Environmental Toxicology Center and  School of Pharmacy, University of Wisconsin, Madison, Wisconsin 53706 and the ^§ Department of Biology, Woods Hole Oceanographic Institution, Woods Hole, Massachusetts 02543

Two aryl hydrocarbon receptors (AhRs), rtAhR2 and rtAhR2, were cloned from rainbow trout (rt) cDNA libraries. The distribution of sequence differences, genomic Southern blot analysis, and the presence of both transcripts in all individual rainbow trout examined suggest that the two forms of rtAhR2 are derived from separate genes. The two rtAhR2s have significant sequence similarity with AhRs cloned from mammalian species, especially in the basic helix-loop-helix and PAS functional domains located in the amino-terminal 400 amino acids of the protein. In contrast, the Gln-rich transactivation domain found in the carboxyl-terminal half of mammalian AhRs is absent from both rtAhR2s. Both clones were expressed by in vitro transcription/translation and proteins of approximately 125 kDa were produced. These proteins bind 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) and are able to bind dioxin response elements in gel shift assays. rtAhR2 and rtAhR2 are expressed in a tissue-specific manner with the highest expression of rtAhR2 in the heart. Expression of rtAhR2 and rtAhR2 mRNAs is positively regulated by TCDD. Both rtAhR2 and rtAhR2 produced TCDD-dependent activation of a reporter gene driven by dioxin response elements. Surprisingly, the two receptors showed distinct preferences for different enhancer sequences. These results suggest that the two receptor forms may regulate different sets of genes, and may play different roles in the toxic responses produced by AhR agonists such as TCDD.

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