DNA sequence-specific binding of transformed ah receptor to a dioxin responsive enhancer: Looks aren't everything

M. S. Denison, P. A. Bank, E. F. Yao

Research output: Contribution to journalArticle

Abstract

Gel retardation analysis has been utilized to examine the ability of transformed hepatic cytosolic TCDD:AhR complex to bind to its specific DNA recognition site, the dioxin responsive element (DRE). Although DRE sequence alignment has identified a conserved DNA recognition sequence of C/GNNNC/GTNGCGTGNC/GT/ANNNC/G, site-directed mutagenesis has demonstrated that not all of these bases are important for DNA binding. A putative TCDD:AhR DRE-binding consensus of GCGTGNNA/TNNNG/C has been derived from our studies and it is highly conserved among species. In addition, we present a model for the DNA-binding of transformed TCDD:AhR complex.

Original languageEnglish (US)
Pages (from-to)33-36
Number of pages4
JournalChemosphere
Volume25
Issue number1-2
DOIs
StatePublished - 1992
Externally publishedYes

Fingerprint

Dioxins
DNA sequences
dioxin
TCDD
DNA
Sequence Alignment
Site-Directed Mutagenesis
Mutagenesis
Gels
gel
Liver
Polychlorinated Dibenzodioxins

ASJC Scopus subject areas

  • Environmental Science(all)
  • Environmental Chemistry

Cite this

DNA sequence-specific binding of transformed ah receptor to a dioxin responsive enhancer : Looks aren't everything. / Denison, M. S.; Bank, P. A.; Yao, E. F.

In: Chemosphere, Vol. 25, No. 1-2, 1992, p. 33-36.

Research output: Contribution to journalArticle

Denison, M. S. ; Bank, P. A. ; Yao, E. F. / DNA sequence-specific binding of transformed ah receptor to a dioxin responsive enhancer : Looks aren't everything. In: Chemosphere. 1992 ; Vol. 25, No. 1-2. pp. 33-36.
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