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

doi:10.1016/0045-6535(92)90473-5

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 journal › Article › peer-review

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 language	English (US)
Pages (from-to)	33-36
Number of pages	4
Journal	Chemosphere
Volume	25
Issue number	1-2
DOIs	https://doi.org/10.1016/0045-6535(92)90473-5
State	Published - 1992
Externally published	Yes

ASJC Scopus subject areas

Environmental Science(all)
Environmental Chemistry

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

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.",

author = "Denison, {M. S.} and Bank, {P. A.} and Yao, {E. F.}",

year = "1992",

doi = "10.1016/0045-6535(92)90473-5",

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T1 - DNA sequence-specific binding of transformed ah receptor to a dioxin responsive enhancer

T2 - Looks aren't everything

AU - Denison, M. S.

AU - Bank, P. A.

AU - Yao, E. F.

PY - 1992

Y1 - 1992

N2 - 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.

AB - 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.

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JF - Chemosphere

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

Abstract

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