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 | |
| State | Published - 1992 |
| Externally published | Yes |
Fingerprint
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 journal › Article
}
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 -