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Originally published In Press as doi:10.1074/jbc.M006048200 on July 31, 2000

J. Biol. Chem., Vol. 275, Issue 40, 30977-30986, October 6, 2000
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The Pit-1beta Domain Dictates Active Repression and Alteration of Histone Acetylation of the Proximal Prolactin Promoter*

Scott E. DiamondDagger and Arthur Gutierrez-Hartmann§

From the § Department of Medicine and Department of Biochemistry and Molecular Genetics, Program in Molecular Biology and Colorado Cancer Center, University of Colorado Health Sciences Center, Denver, Colorado 80262

A critical problem in current molecular biology is to gain a detailed understanding of the molecular mechanisms by which related transcription factor isoforms with identical DNA sequence specificity mediate distinct transcription responses. Pit-1 and Pit-1beta constitute such a pair of transcription factor isoforms. Pit-1 enhances the Ras signaling pathway to the prolactin promoter, and Pit-1beta represses basal prolactin promoter activity as well as Ras signaling to the prolactin promoter in pituitary cells. We have previously demonstrated that the beta -domain amino acid sequence dictates the transcriptional properties of Pit-1beta . Here, we show that five hydrophobic beta -domain residues are required for Pit-1 isoform-specific repression of Ras signaling, and we demonstrate that sodium butyrate and trichostatin A, pharmacological inhibitors of histone deacetylation, as well as viral Ski protein, a dominant-negative inhibitor of recruitment of N-CoR/mSin3 histone deacetylase complexes, specifically reverse beta  isoform-specific repression of Ras signaling. Moreover, we directly demonstrate, with a chromatin immunoprecipitation assay, that the Pit-1beta isoform alters the histone acetylation state of the proximal prolactin promoter. This differential analysis of Pit-1/Pit-1beta isoform function provides significant insights into the structural determinants that govern how different transcription factors with identical DNA sequence specificity can display opposite effects on target gene activity.

* This work was supported in part by National Institutes of Health Grant R01 DK37667 (to A. G.-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 Supported by a postdoctoral fellowship from the Lalor Foundation, a University of Colorado Cancer Center research seed grant, and National Institutes of Health Mentored Research Scientist Development Award K01 DK02752-01. Present address: Dept. of Physiology, University of Kentucky College of Medicine, MS-508 Albert B. Chandler Medical Center, 800 Rose St., Lexington, KY 40536-0298.

To whom correspondence should be addressed: Depts. of Medicine and of Biochemistry and Molecular Genetics, Program in Molecular Biology, Colorado Cancer Center, 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 © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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