scholarly journals Abnormal Liver Development and Resistance to 2,3,7,8-Tetrachlorodibenzo-p-Dioxin Toxicity in Mice Carrying a Mutation in the DNA-Binding Domain of the Aryl Hydrocarbon Receptor

2008 ◽  
Vol 106 (1) ◽  
pp. 83-92 ◽  
Author(s):  
Maureen K. Bunger ◽  
Edward Glover ◽  
Susan M. Moran ◽  
Jacqueline A. Walisser ◽  
Garet P. Lahvis ◽  
...  
Keyword(s):  
Dna Binding ◽  
Aryl Hydrocarbon Receptor ◽  
Binding Domain ◽  
Liver Development ◽  
Dna Binding Domain ◽  
Aryl Hydrocarbon ◽  
Tetrachlorodibenzo P Dioxin ◽  
Dioxin Toxicity

scholarly journals Transformation of the aryl hydrocarbon receptor to a DNA-binding form is accompanied by release of the 90 kDa heat-shock protein and increased affinity for 2,3,7,8-tetrachlorodibenzo-p-dioxin

1993 ◽  
Vol 294 (1) ◽  
pp. 95-101 ◽  
Author(s):  
E C Henry ◽  
T A Gasiewicz
Keyword(s):  
Heat Shock ◽  
Dna Binding ◽  
Heat Shock Protein ◽  
Aryl Hydrocarbon Receptor ◽  
Incubation Temperature ◽  
Binding Affinities ◽  
Aryl Hydrocarbon ◽  
Molecular Events ◽  
Binding Forms ◽  
Tetrachlorodibenzo P Dioxin

The binding of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) to the aryl hydrocarbon receptor (AhR) elicits a sequence of poorly defined molecular events that ultimately yield a heteromeric transformed AhR that is active as a transcription factor. We have previously developed a model of the ligand-initiated transformation of the AhR to the DNA-binding state based on characterization of several forms of the AhR with respect to their physicochemical properties and DNA-binding affinities. The present studies were designed to determine whether, and at what stage, this process of transformation alters the receptor's affinity for TCDD. In rat hepatic cytosol, approx. 10% of the TCDD specifically bound to the AhR rapidly dissociated (t1/2 approximately 1 h), while the remainder was only slowly dissociable (t1/2 approximately 70 h). The isolated DNA-binding forms of the receptor (monomeric and transformed) bound TCDD very tightly (t1/2 > 100 h), whereas TCDD was dissociable from the non-DNA-binding receptor form(s). A lower incubation temperature (0-4 degrees C) and the presence of molybdate partially stabilized the non-DNA-binding fraction of the TCDD.receptor complex and also enhanced TCDD dissociation in crude cytosol. Immunoprecipitation of the different AhR forms with an anti-AhR antibody and immunoblotting with antibody to the 90 kDa heat-shock protein (hsp90) demonstrated that hsp90 was associated with the unoccupied receptor complex as well as with a fraction of the non-DNA-binding TCDD.receptor complex; isolated DNA-binding forms did not contain detectable hsp90. We conclude that while hsp90 remains associated with the AhR, TCDD is readily dissociable; following release of hsp90, however, TCDD becomes very tightly bound, and remains so upon completion of transformation.

scholarly journals Nucleoside triphosphates promote the transformation of Ah receptor to its DNA-binding form

1991 ◽  
Vol 274 (2) ◽  
pp. 401-404 ◽  
Author(s):  
A J Cary ◽  
J J Dougherty
Keyword(s):  
Dna Binding ◽  
Aryl Hydrocarbon Receptor ◽  
Ah Receptor ◽  
Nucleotide Hydrolysis ◽  
Aryl Hydrocarbon ◽  
Low Concentrations ◽  
Nucleoside Triphosphates ◽  
Tetrachlorodibenzo P Dioxin ◽  
Specific Ligand

When it is bound to a specific ligand such as 2,3,7,8-tetrachlorodibenzo-p-dioxin, mild heating can convert the Ah (aryl hydrocarbon) receptor into a form capable of binding DNA. We found that physiological (1-3 mM) levels of ATP substantially increased the transformation of the receptor to its DNA-binding form. GTP, UTP and CTP had similar effects. ADP also promoted this transformation, but was less effective than ATP at low concentrations. Pyrophosphate too promoted transformation, but AMP had little effect. The process did not require nucleotide hydrolysis, since non-hydrolysable analogues of ATP such as adenosine 5′-[beta gamma-imido]triphosphate were nearly as effective as ATP itself. Inhibitors of ATP-stimulated proteases did not significantly affect the ability of ATP to promote receptor transformation, which suggests that the effect of ATP was not mediated by these proteases.

NMR studies of the R2 repeat and related peptide fragments of the DNA binding domain of c-Myb. New light on the structure and folding of R2.

1999 ◽  
Vol 96 (9/10) ◽  
pp. 1580-1584 ◽  
Author(s):  
I. Ségalas ◽  
S. Desjardins ◽  
H. Oulyadi ◽  
Y. Prigent ◽  
S. Tribouillard ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Peptide Fragments ◽  
Nmr Studies ◽  
Related Peptide

scholarly journals Primary structure of a glycosylated DNA-binding domain in human plasma fibronectin.

1985 ◽  
Vol 260 (4) ◽  
pp. 2301-2306
Author(s):  
H Pande ◽  
J Calaycay ◽  
D Hawke ◽  
C M Ben-Avram ◽  
J E Shively
Keyword(s):  
Dna Binding ◽  
Human Plasma ◽  
Primary Structure ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Plasma Fibronectin
Sign in / Sign up

Export Citation Format

Share Document