Association of the Drosophila melanogaster engrailed protein with specific soluble nuclear protein complexes
| Autor: | Gay, N J, Poole, S, Kornberg, T |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Biology
DNA-binding protein General Biochemistry Genetics and Molecular Biology chemistry.chemical_compound Animals Nuclear protein Molecular Biology Gene Cell Line Transformed Regulation of gene expression General Immunology and Microbiology General Neuroscience Genes Homeobox Nuclear Proteins biology.organism_classification Molecular biology engrailed Cell biology DNA-Binding Proteins Molecular Weight Drosophila melanogaster Gene Expression Regulation Solubility chemistry Homeobox DNA Research Article |
| Zdroj: | The EMBO Journal. 7:4291-4297 |
| ISSN: | 0261-4189 |
| DOI: | 10.1002/j.1460-2075.1988.tb03327.x |
| Popis: | The Drosophila engrailed protein which contains a homeobox domain and specific DNA binding activity is believed to function in the regulation of gene expression during embryogenesis. Here we show that the engrailed protein interacts stably with specific complexes of soluble nuclear proteins when expressed artificially in a cell line and in the developing embryo. The engrailed complexes have molecular masses between 10(7) and 10(8) which suggests they contain a polymeric protein component. The complex is able to bind reversibly to DNA and a definitive purification shows it to be constituted of 12 distinct protein species, two of which are predominant. Purified, bacterially produced engrailed protein can be reconstituted with both culture cell and embryo nuclear protein fractions to form complexes of the same and related composition respectively. On the basis of these results we propose that protein--protein interactions as well as DNA binding are important for correct engrailed protein function in vivo. |
| Databáze: | OpenAIRE |
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