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Originally published In Press as doi:10.1074/jbc.M213063200 on March 4, 2003

J. Biol. Chem., Vol. 278, Issue 19, 16863-16872, May 9, 2003
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Purification and Mass Spectrometric Identification of GA-binding Protein (GABP) as the Functional Pituitary Ets Factor Binding to the Basal Transcription Element of the Prolactin Promoter*

Rebecca E. SchweppeDagger §, Alexis A. Melton, Kelley S. Brodsky, Lauren D. Aveline||, Katheryn A. Resing**, Natalie G. Ahn||**, and Arthur Gutierrez-HartmannDagger Dagger Dagger

From the  Department of Medicine and Dagger  Department of Biochemistry and Molecular Genetics, Program in Molecular Biology, and Colorado Cancer Center, University of Colorado Health Sciences Center, Denver, Colorado 80262 and the ** Department of Chemistry and Biochemistry, and || Howard Hughes Medical Institute, University of Colorado, Boulder, Colorado 80309

The Ets-binding site within the basal transcription element (BTE) of the rat prolactin (rPRL) promoter is critical for both basal and growth factor-regulated rPRL gene expression. Here we report the purification and identification of the factor that binds to the BTE. This factor was purified from GH3 pituitary nuclear extracts using ammonium sulfate fractionation, heparin-Sepharose and Mono Q chromatography, and BTE-affinity magnetic beads. We purified two proteins of 57 and 47 kDa and identified the 57-kDa protein by mass spectrometry as the Ets factor GABPalpha . Western blot analysis identified the 47-kDa protein as GABPbeta 1. Co-transfection of dominant-negative GABPbeta 1 blocks prolactin promoter basal activity by 85-88% in GH3 cells in the presence or absence of FGF-4. Additionally, expression of wild-type GABPalpha /beta 1 selectively activates a minimal BTE promoter 24-28-fold in GH3 cells, and this activation is dependent on the Ets-binding site. Finally, small interfering RNA depletion of GABP in GH3 cells results in the loss of prolactin protein. Thus, we have identified GABPalpha /GABPbeta 1 as a critical and functionally relevant Ets factor that regulates rPRL promoter activity via the BTE site.

* This work was supported by National Institutes of Health Grants DK46868 (to A. G. H.) and AR39730 (to K. A. R.).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.

§ Present address: Dept. of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309.

Dagger Dagger To whom correspondence should be addressed: University of Colorado Health Sciences Center, 4200 East Ninth Ave., Box B-151, Denver, CO 80262. Tel.: 303-315-8443; Fax: 303-315-4525; E-mail: a.gutierrez-hartmann@uchsc.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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