Abstract
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.
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Dates
Type | When |
---|---|
Created | 18 years, 2 months ago (June 5, 2007, 5:15 p.m.) |
Deposited | 3 years, 9 months ago (Nov. 13, 2021, 11:02 p.m.) |
Indexed | 11 months, 4 weeks ago (Sept. 5, 2024, 1:52 p.m.) |
Issued | 35 years, 11 months ago (Oct. 1, 1989) |
Published | 35 years, 11 months ago (Oct. 1, 1989) |
Published Online | 35 years, 11 months ago (Oct. 1, 1989) |
Published Print | 35 years, 11 months ago (Oct. 1, 1989) |
@article{Roux_1989, title={The cell-specific transcription factor PTF1 contains two different subunits that interact with the DNA.}, volume={3}, ISSN={1549-5477}, url={http://dx.doi.org/10.1101/gad.3.10.1613}, DOI={10.1101/gad.3.10.1613}, number={10}, journal={Genes & Development}, publisher={Cold Spring Harbor Laboratory}, author={Roux, E and Strubin, M and Hagenbüchle, O and Wellauer, P K}, year={1989}, month=oct, pages={1613–1624} }