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

Access to Document

10.1016/0045-6535(92)90473-5

Fingerprint Dive into the research topics of 'DNA sequence-specific binding of transformed ah receptor to a dioxin responsive enhancer: Looks aren't everything'. Together they form a unique fingerprint.

Cite this

@article{da073eee7a994477a0416dec42605cd9,

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",

language = "English (US)",

volume = "25",

pages = "33--36",

journal = "Chemosphere",

issn = "0045-6535",

publisher = "Elsevier Limited",

number = "1-2",

}

TY - JOUR

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.

UR - http://www.scopus.com/inward/record.url?scp=0026726437&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026726437&partnerID=8YFLogxK

U2 - 10.1016/0045-6535(92)90473-5

DO - 10.1016/0045-6535(92)90473-5

M3 - Article

AN - SCOPUS:0026726437

VL - 25

SP - 33

EP - 36

JO - Chemosphere

JF - Chemosphere

SN - 0045-6535

IS - 1-2

ER -