The cell-specific transcription factor PTF1 contains two different subunits that interact with the DNA
| Autor: | Michel Strubin, E Roux, Peter K. Wellauer, O Hagenbüchle |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
HMG-box
Ultraviolet Rays Base pair Molecular Sequence Data In Vitro Techniques Biology Chromatography Affinity chemistry.chemical_compound Genetics Animals Protein–DNA interaction DNA clamp Base Sequence Molecular Structure DNA DNA-binding domain Rats DNA binding site Cross-Linking Reagents Biochemistry chemistry DNA construct alpha-Amylases DNA Probes Protein Binding Transcription Factors Developmental Biology |
| Zdroj: | Genes & Development. 3:1613-1624 |
| ISSN: | 1549-5477 0890-9369 |
| DOI: | 10.1101/gad.3.10.1613 |
| Popis: | The cognate sequence of transcription factor PTF1, which plays a key role in pancreas-specific gene expression, has a bipartite organization. Two separate DNA domains, the A and the B boxes, are required for efficient binding of the factor. The structure of PTF1 was elucidated by cross-linking purified PTF1 to DNA templates that had been differentially substituted with azido-deoxyuridine (N3.dU). This site-directed UV cross-linking shows that PTF1 contains two DNA-binding proteins, distinct in size and sensitivity to Staphylococcus aureus V8 protease. A 64-kD protein is cross-linked with DNA containing N3.dU substitutions in the A box, and a 48-kD protein is cross-linked with DNA containing N3.dU substitutions in the B box. Both proteins bind simultaneously to the same DNA molecule. The data indicate that PTF1 is a heteromeric oligomer and that its cell-specific DNA-binding potential is the result of a concerted activity of two DNA-binding subunits. |
| Databáze: | OpenAIRE |
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