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 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Protein-DNA interactions at recognition sites for the dioxin-Ah receptor complex. / Denison, M. S.; Fisher, J. M.; Whitlock, J. P.
In: Journal of Biological Chemistry, Vol. 264, No. 28, 1989, p. 16478-16482.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Protein-DNA interactions at recognition sites for the dioxin-Ah receptor complex
AU - Denison, M. S.
AU - Fisher, J. M.
AU - Whitlock, J. P.
PY - 1989
Y1 - 1989
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0024462025&partnerID=8YFLogxK
M3 - Article
C2 - 2550446
AN - SCOPUS:0024462025
VL - 264
SP - 16478
EP - 16482
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 28
ER -