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

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

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

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

Research output: Contribution to journal › Article › peer-review

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

ASJC Scopus subject areas

Biochemistry

Fingerprint Dive into the research topics of 'Protein-DNA interactions at recognition sites for the dioxin-Ah receptor complex'. Together they form a unique fingerprint.

Cite this

@article{bcd8d1f9e0214c23a57af0bc20fd6ecb,

title = "Protein-DNA interactions at recognition sites for the dioxin-Ah receptor complex",

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.",

author = "Denison, {M. S.} and Fisher, {J. M.} and Whitlock, {J. P.}",

year = "1989",

language = "English (US)",

volume = "264",

pages = "16478--16482",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "28",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=0024462025&partnerID=8YFLogxK

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 -