Abstract
We show that the Drosophila protein DSP1, an HMG-1/2-like protein, binds DNA highly cooperatively with three members of the Rel family of transcriptional regulators (NF-κB, the p50 subunit of NF-κB, and the Rel domain of Dorsal). This cooperativity is apparent with DNA molecules bearing consensus Rel-protein-binding sites and is unaffected by the presence of a negative regulatory element, a sequence previously proposed to be important for mediating repression by these Rel proteins. The cooperativity observed in these DNA-binding assays is paralleled by interactions between protein pairs in the absence of DNA. We also show that in HeLa cells, as assayed by transient transfection, expression of DSP1 increases activation by Dorsal from the twist promoter and inhibits that activation from the zen promoter, consistent with the previously proposed idea that DSP1 can affect the action of Dorsal in a promoter-specific fashion.
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Dates
Type | When |
---|---|
Created | 23 years ago (July 26, 2002, 10:40 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 3:28 p.m.) |
Indexed | 1 year, 1 month ago (July 13, 2024, 5:14 p.m.) |
Issued | 25 years, 11 months ago (Sept. 14, 1999) |
Published | 25 years, 11 months ago (Sept. 14, 1999) |
Published Online | 25 years, 11 months ago (Sept. 14, 1999) |
Published Print | 25 years, 11 months ago (Sept. 14, 1999) |
@article{Brickman_1999, title={Interactions between an HMG-1 protein and members of the Rel family}, volume={96}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.96.19.10679}, DOI={10.1073/pnas.96.19.10679}, number={19}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Brickman, Joshua M. and Adam, Maryse and Ptashne, Mark}, year={1999}, month=sep, pages={10679–10683} }