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J Biol Chem, Vol. 275, Issue 17, 13082-13088, April 28, 2000

An NF-Y Binding Site Is Important for Basal, but Not Gonadotropin-releasing Hormone-stimulated, Expression of the Luteinizing Hormone beta  Subunit Gene*

Ruth A. Keri, Daniel J. Bachmann, Alireza Behrooz, Brian D. Herr, Rebecca K. Ameduri, Christine C. Quirk, and John H. NilsonDagger

From the Department of Pharmacology, Case Western Reserve University, Cleveland, Ohio 44106

Regulated synthesis of luteinizing hormone (LH) requires coordinated transcriptional control of the alpha  and LHbeta subunits in pituitary gonadotropes. Several cis-acting elements and trans-acting factors have been defined for control of the LHbeta promoter through heterologous cell culture models. In this report, we describe the identification of bipartite NF-Y (CBF/CP1) binding sites within the proximal bovine LHbeta promoter. When multimerized, one of these sites activates the heterologous, minimal HSV thymidine kinase promoter in the gonadotrope-derived cell line alpha T3-1. The functional role of the promoter-distal site in regulating the full-length bovine LHbeta promoter was assessed in vivo using transgenic mice harboring a mutant promoter linked to the chloramphenicol acetyltransferase reporter gene. While this element is important for conferring high level activity of the LHbeta promoter in pituitary, it does not appear to be essential for mediating gonadotropin-releasing hormone (GnRH) regulation. This is the first characterization of a cis-acting element within this GnRH-dependent promoter that is restricted to regulating basal expression and not GnRH-induced activity.

* This work was supported by National Institutes of Health Grants DK28559 (to J. H. N.) and DK09843 (to C. C. Q.) and an Endocrine Society fellowship (to B. D. H.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Pharmacology, Case Western Reserve University School of Medicine, 2109 Adelbert Rd., Cleveland, OH 44106. Tel.: 216-368-4497; Fax: 216-368-3395; E-mail: jhn@po.cwru.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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