Protein-DNA interactions at recognition sites for the dioxin-Ah receptor complex

M. S. Denison, J. M. Fisher, J. P. Whitlock

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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 languageEnglish (US)
Pages (from-to)16478-16482
Number of pages5
JournalJournal of Biological Chemistry
Volume264
Issue number28
StatePublished - 1989
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry

Cite this

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.