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PMID:1280827
Citation |
Christianson, AM, King, DL, Hatzivassiliou, E, Casas, JE, Hallenbeck, PL, Nikodem, VM, Mitsialis, SA and Kafatos, FC (1992) DNA binding and heteromerization of the Drosophila transcription factor chorion factor 1/ultraspiracle. Proc. Natl. Acad. Sci. U.S.A. 89:11503-7 |
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Abstract |
The Drosophila chorion factor 1/ultraspiracle (CF1/USP) transcription factor, a homologue of the retinoid X receptor, is a developmentally important member of the family of nuclear (steroid) hormone receptors. Using newly developed monoclonal antibodies and a full-length bacterially produced protein, we have studied in detail the in vitro DNA-binding properties of this factor and aspects of its distribution in vivo. During oogenesis, CF1/USP is present both in germline cells and in the somatic follicular epithelium. We have determined the optimal binding site of partially purified bacterially produced CF1/USP by an in vitro selection procedure and also have characterized its binding to the follicular-specific chorion s15 promoter. In vitro this bacterially produced factor is unusual in binding to a single element ("half-site"); simultaneous but noncoordinate binding to a second half-site is possible if these repeated elements are organized in direct orientation and spaced adequately. However, the factor interacts synergistically with several other nuclear hormone receptors: notably, it can form in vitro heteromers with mammalian thyroid and retinoic acid receptors, binding to two half-sites that are organized in either direct or inverted orientation. In vivo the factor most probably functions as a heterodimer, but its partner(s) remains to be determined. |
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Keywords |
Animals; Antibodies, Monoclonal/immunology; Base Sequence; Carrier Proteins/metabolism; Cloning, Molecular; DNA-Binding Proteins/metabolism; Drosophila Proteins; Drosophila melanogaster; Epitopes; Female; Macromolecular Substances; Molecular Sequence Data; Oligodeoxyribonucleotides/chemistry; Ovary/metabolism; Polymerase Chain Reaction; Promoter Regions, Genetic; Protein Binding; Receptors, Retinoic Acid; Receptors, Steroid/metabolism; Receptors, Thyroid Hormone/metabolism; Structure-Activity Relationship; Transcription Factors/metabolism |
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