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Papers In Press, published online ahead of print May 14, 2002
J. Biol. Chem, 10.1074/jbc.M203645200
Submitted on April 15, 2002
Revised on May 9, 2002
Accepted on May 14, 2002
results in synergistic activation of the human lactase-phlorizin hydrolase promoter
Department of Medicine/GI, Children's Hospital, Harvard Medical School, Boston, MA 02115
Corresponding Author: Stephen.krasinski{at}tch.harvard.edu
GATA-4, -5, and -6 zinc finger and HNF-1
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-1 physically associate both in vivo and in vitro, and that this interaction is necessary for cooperative activation of the lactase-phlorizin hydrolase (LPH) promoter. Further, physical association is mediated by the C-terminal zinc finger of GATA factors and the homeodomain of HNF-1. Deletion of HNF-1 activation domains or interruption of HNF-1 binding sites in the LPH promoter results in a complete loss of cooperativity, whereas deletion of GATA-5 activation domains or interruption of GATA binding sites results in a reduction, but not an elimination of cooperativity. We hypothesize that GATA/HNF-1-cooperativity is mediated by HNF-1through 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 co-expressed in the intestine. Parallel mechanisms in other tissue 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.
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