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Vol. 62, Issue 2, 234-249, August 2002
Environmental Toxicology Center (E.A.A., W.H., R.E.P.) and School
of Pharmacy (W.H., R.E.P.), University of Wisconsin, Madison,
Wisconsin; Biology Department (M.E.H.), Woods Hole Oceanographic
Institution, Woods Hole, Massachusetts; and Department of
Pharmaceutical Sciences (R.L.T.), School of Pharmacy, University of
Colorado Health Sciences Center, Denver, Colorado
Fish are known to have two distinct classes of aryl hydrocarbon
receptors, and their roles in mediating xenobiotic toxicity remain
unclear. In this study, we have identified and characterized a cDNA
tentatively named zebrafish AHR1 (zfAHR1). Analysis of the deduced amino acid sequence reveals that the protein is distinct from zfAHR2 and is more closely related to the mammalian aryl hydrocarbon receptor (AHR). zfAHR1 and zfAHR2 share 40% amino acid
identity overall and 58% in the N-terminal half. The
zfAHR1 gene maps to linkage group 16 in a region that
shares conserved synteny with human chromosome 7 containing the human
AHR, suggesting that the zfAHR1 is the
ortholog of the human AHR. zfAHR2 maps to a separate
linkage group (LG22). Both zfAHR mRNAs are expressed in early
development, but they are differentially expressed in adult tissues.
zfAHR2 can dimerize with zfARNT2b and binds with specificity to
dioxin-responsive elements (DREs). Under identical conditions,
zfAHR1/zfARNT2b/DRE complexes are formed; however, the interactions are
considerably weaker. In COS-7 cells expressing zfARNT2b and zfAHR2,
2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) exposure
leads to a significant induction of dioxin-responsive reporter genes.
In identical experiments, TCDD exposure fails to induce the reporter
gene in zfAHR1-expressing cells. Ligand-binding experiments suggested
that the differential zfAHR activities are attributable to differences
in TCDD binding because only zfAHR2 exhibits high-affinity binding to
[3H]TCDD or 
-naphthoflavone. Finally, using chimeric
zfAHR1/zfAHR2 constructs, the lack of TCDD-mediated transcriptional
activity was localized to the ligand-binding and C-terminal domains of zfAHR1.
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