The nuclear hormone receptor Ftz-F1 is a cofactor for the Drosophila homeodomain protein Ftz

Yan Yu, Willis Li, Kai Su, Miyuki Yussa, Wei Han, Norbert Perrimon and Leslie Pick
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Yan Yu: Mount Sinai School of Medicine
Willis Li: Harvard Medical School
Kai Su: Mount Sinai School of Medicine
Miyuki Yussa: Mount Sinai School of Medicine
Wei Han: Mount Sinai School of Medicine
Norbert Perrimon: Harvard Medical School
Leslie Pick: Mount Sinai School of Medicine

Nature, 1997, vol. 385, issue 6616, 552-555

Abstract: Abstract Homeobox genes specify cell fate and positional identity in embryos throughout the animal kingdom1. Paradoxically, although each has a specific function in vivo, the in vitro DNA-binding specificities of homeodomain proteins are overlapping and relatively weak. A current model is that homeodomain proteins interact with cofactors that increase specificity in vivo2,3. Here we use a native binding site for the homeodomain protein Fushi tarazu (Ftz) to isolate Ftz-Fl, a protein of the nuclear hormone-receptor superfamily and a new Ftz cofactor. Ftz and Ftz-Fl are present in a complex in Drosophila embryos. Ftz-Fl facilitates the binding of Ftz to DNA, allowing interactions with weak-affinity sites at concentrations of Ftz that alone bind only high-affinity sites. Embryos lacking Ftz-Fl display ftz-like pair-rule cuticular defects. This phenotype is a result of abnormal ftz function because it is expressed but fails to activate downstream target genes. Cooperative interaction between homeodomain proteins and cofactors of different classes may serve as a general mechanism to increase HOX protein specificity and to broaden the range of target sites they regulate.

Date: 1997
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DOI: 10.1038/385552a0

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