Journal
CELL
Volume 129, Issue 6, Pages 1111-1123Publisher
CELL PRESS
DOI: 10.1016/j.cell.2007.05.019
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Funding
- NIAID NIH HHS [R01AI020642, R01 AI020642-23, R01 AI020642] Funding Source: Medline
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Transcriptional activation of the interferon-beta (IFN-beta) gene requires assembly of an enhanceo-some containing ATF-2/c-Jun, IRF-3/IRF-7, and NF kappa B. These factors bind cooperatively to the IFN-beta enhancer and recruit coactivators and chromatin-remodeling proteins to the IFN-beta promoter. We describe here a crystal structure of the DNA-binding domains of IRF-3, IRF-7, and NF kappa B, bound to one half of the enhancer, and use a previously described structure of the remaining half to assemble a complete picture of enhanceosome architecture in the vicinity of the DNA. Association of eight proteins with the enhancer creates a continuous surface for recognizing a composite DNA-binding element. Paucity of local protein-protein contacts suggests that cooperative occupancy of the enhancer comes from both binding-induced changes in DNA conformation and interactions with additional components such as CBP. Contacts with virtually every nucleotide pair account for the evolutionary invariance of the enhancer sequence.
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