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Submitted on August 19, 2002
Accepted on December 31, 2002
1 Department of Biology, Indiana University, Bloomington, Indiana 47405-3700
* To whom correspondence should be addressed. E-mail: cherbas{at}indiana.edu.
The ecdysone receptor is a heterodimer of the two nuclear receptors EcR and USP. We have identified the regions of Drosophila EcR and USP responsible for transcriptional activation of a semi-synthetic Eip71CD promoter in Kc cells. The isoform-specific A/B domains of EcR-B1 and B2 but not those of EcR-A or USP exhibit strong activation activity (AF1), both in isolation and in the context of the intact receptor. AF1 activity in isoform B1 derives from dispersed elements; the B2-specific AF1 consists of a 17-residue amphipathic helix. AF2 function was studied using a two-hybrid assay in Kc cells, based on the observation that potent hormone-dependent activation by the EcR/USP LBD heterodimer requires the participation of both partners. Mutagenesis reveals that AF2 function depends on EcR helix 12, but not on the cognate USP region. EcR helix 12 mutants (F645A and W650A) exhibit a dominant negative phenotype. Thus, in the setting tested, the ecdysone receptor can activate transcription using the AF1 regions of EcR-B1 or -B2 and the AF2 region of EcR. USP acts as an allosteric effector for EcR, but does not contribute any intrinsic function.
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