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J. Biol. Chem., Vol. 269, Issue 48, 30109-30112, 12, 1994
LA Carver, V Jackiw and CA Bradfield
In an effort to provide a more powerful system to study the Ah receptor
(AHR) signaling pathway, we expressed the AHR, its dimerization partner
ARNT, and a beta-galactosidase (lacZ) reporter gene, driven by two
dioxin-responsive enhancers, in the yeast Saccharomyces cerevisiae. In this
system, the agonists beta-naphthoflavone and alpha-naphthoflavone induced
transcription of the lacZ gene, with EC50 values of 7.9 x 10(- 8) and 3.0 x
10(-7) M, respectively, while the nonagonist dexamethasone was without
effect. As a first application of this system, we examined the relationship
between the 90-kDa heat shock protein (hsp90) and AHR function. To
accomplish this in a manner that was independent of the ARNT protein, we
constructed a chimeric receptor in which the DNA binding and primary
dimerization domains of the AHR were swapped with analogous domains from
the LexA protein. Coexpression of this AHR-LexA chimera and a lacZ reporter
gene driven by eight LexA operator sites in a yeast strain with regulatable
levels of hsp90, yielded pharmacology that closely mirrored that of the
AHR/ARNT/dioxin-responsive enhancer system described above, but only when
hsp90 levels were held near their wild type levels. When hsp90 levels were
reduced to approximately 5% of normal, AHR signaling in response to agonist
was completely blocked despite normal cell growth. These results provide
the first genetic evidence for the role of hsp90 in AHR signaling and
provide the basis for a powerful new system in which to study this pathway.
The 90-kDa heat shock protein is essential for Ah receptor signaling in a yeast expression system
Department of Molecular Pharmacology and Biological Chemistry, Northwestern University Medical School, Chicago, Illinois 60611.
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