Abstract
Gel retardation analyses reveal a cluster of six binding sites for the liganded Ah receptor within a 700-base pair DNA domain upstream of the mouse CYP 1A1 gene. The nucleotide sequences of the binding sites define a consensus recognition motif for the liganded receptor. The consensus motif is not symmetric. Alteration of the consensus motif produces a decrease in the receptor-DNA interaction. The liganded receptor binds as a monomer to its recognition motif and preferentially binds to double-stranded DNA. These observations reveal apparent differences between 2,3,7,8-tetrachlorodibenzo-p-dioxin and steroid hormones in their respective mechanisms of action.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 16478-16482 |
| Number of pages | 5 |
| Journal | Journal of Biological Chemistry |
| Volume | 264 |
| Issue number | 28 |
| State | Published - 1989 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
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Denison, M. S., Fisher, J. M., & Whitlock, J. P. (1989). Protein-DNA interactions at recognition sites for the dioxin-Ah receptor complex. Journal of Biological Chemistry, 264(28), 16478-16482.