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Originally published In Press as doi:10.1074/jbc.M203645200 on May 14, 2002

J. Biol. Chem., Vol. 277, Issue 31, 27659-27667, August 2, 2002
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Physical Interaction between GATA-5 and Hepatocyte Nuclear Factor-1alpha Results in Synergistic Activation of the Human Lactase-Phlorizin Hydrolase Promoter*

Herbert M. van WeringDagger §||, Inge L. HuibregtseDagger Dagger , Sanne M. van der ZwanDagger Dagger , Maartje S. de BieDagger ||, Lauren N. DowlingDagger , François Boudreau**, Edmond H. H. M. Rings**, Richard J. GrandDagger §, and Stephen D. KrasinskiDagger §§§¶¶

From the Dagger  Division of Gastroenterology and Nutrition, Department of Medicine, Children's Hospital, Boston, Massachusetts 02115, the § Department of Pediatrics, Harvard Medical School, Boston, Massachusetts 02115, the  Department of Pediatrics, New England Medical Center, Boston, Massachusetts 02111, the §§ Gerald J. and Dorothy R. Friedman School of Nutrition Science and Policy, Tufts University, Medford, Massachusetts 02155, the ** Division of Gastroenterology, Department of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, the || Department of Medicine, Free University of Amsterdam, Amsterdam, The Netherlands 1081HV, and the Dagger Dagger  Department of Medicine, University of Amsterdam, Amsterdam, The Netherlands 1100DD

GATA-4, -5, and -6 zinc finger and hepatocyte nuclear factor-1alpha (HNF-1alpha ) homeodomain transcription factors are expressed in the intestinal epithelium and synergistically activate the promoter of intestinal genes. Here, we demonstrate that GATA-5 and HNF-1alpha physically associate both in vivo and in vitro and that this interaction is necessary for cooperative activation of the lactase-phlorizin hydrolase promoter. Furthermore, physical association is mediated by the C-terminal zinc finger of GATA factors and the homeodomain of HNF-1alpha . Deletion of HNF-1alpha activation domains or interruption of HNF-1-binding sites in the lactase-phlorizin hydrolase promoter resulted in a complete loss of cooperativity, whereas deletion of GATA-5 activation domains or interruption of GATA-binding sites resulted in a reduction, but not an elimination, of cooperativity. We hypothesize that GATA/HNF-1alpha cooperativity is mediated by HNF-1alpha through its activation domains, which are oriented for high levels of activation through binding to DNA and physical association with GATA factors. These data suggest a paradigm whereby intestine-specific gene expression is regulated by unique interactions among tissue-restricted transcription factors coexpressed in the intestine. Parallel mechanisms in other tissues as well as in Drosophila suggest that zinc finger/homeodomain interactions are an efficient pathway of cooperative activation of gene transcription that has been conserved throughout evolution.

* This work was supported by NIDDK Grant R37-DK-32658 and Silvio O. Conte Digestive Disease Core Center Grant P30-DK-34928 from the National Institutes of Health, by a grant from the Nutricia Research Foundation (to H. M. v. W.), and by an interim support grant from the New England Medical Center (to S. D. K.).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.

¶¶ To whom correspondence should be addressed: Div. of Gastroenterology and Nutrition, Enders 1220, Children's Hospital, 300 Longwood Ave., Boston, MA 02115. Tel.: 617-355-2222; Fax: 617-264-2876; E-mail: stephen.krasinski@tch.harvard.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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