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Submitted on December 19, 2002
Accepted on March 27, 2003
1 Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, P. O. Box 016129, Miami, Florida 33101
* To whom correspondence should be addressed.
This paper describes the structural and functional characterization of Ini (AF495522), a novel highly conserved zinc-finger protein that had been identified by screening an estrogen-induced rat myometrial expression library (1). Ini localizes to the nucleus of HeLa cells and binds to the proximal cx43 promoter, as demonstrated by Electrophoretic Mobility Shift Assay (EMSA). In addition, transient transfection experiments performed with estrogen receptor 
(ER) cDNA show that overexpression of Ini enhances, in a dose-dependent fashion, the up-regulation of the cx43 gene by estrogen. Upon binding to the cx43 promoter Ini stimulates the transcriptional activating function AF-1, but not the AF-2, of the ER. This makes Ini one of the few known coactivators specific for AF-1. Since estrogen upregulates Ini mRNA in the myometrium, it is likely that Ini's physiological role in this tissue is to modulate the response of the cx43 gene to estrogen. Transfection studies with an Ini antisense construct seem to indicate that Ini plays an additional role in the cellular response to estrogen affecting both AF-1 and AF-2 activities of the ER. This broader effect may be associated with cell cycle progression which in yeast has been shown to require Ini (2-3).
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