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J. Biol. Chem., Vol. 269, Issue 44, 27337-27343, 11, 1994
M Ema, N Ohe, M Suzuki, J Mimura, K Sogawa, S Ikawa and Y Fujii-Kuriyama
The genetic difference in the susceptibility of mice to environmental
toxicities induced by dioxin and related chemicals is governed by
polymorphism of the arylhydrocarbon receptor (AhR) (Poland, A., and
Knutson, C. (1982) Annu. Rev. Pharmacol. Toxicol. 22, 517-554). cDNA
cloning of AhR cDNA from responder (C57BL/6) and non-responder (DBA/2J)
mice allowed us to analyze the structure and function of these AhRs. Both
of the AhRs, which were expressed in COS-7 cells transfected with their
expression plasmids, showed a clear 9 S complex with 2,3,7,8-
[3H]tetrachlorodibenzo-p-dioxin (TCDD) in a linear glycerol gradient
centrifugation, consistent with the result of the endogenously expressed
AhR in Hepa-1 cells. This result provides the first direct evidence that
the cDNA-encoded protein binds the ligand specifically. Scatchard plot
analysis revealed that the dissociation constant (Kd) of C57BL AhR for TCDD
is 0.27 nM, while that of DBA AhR is elevated up to six times that high.
Chimeric plasmids between the two cDNAs and site- directed mutagenesis
revealed two critical alterations responsible for the reduced ligand
binding activity: an Ala375 to Val alteration and an elongated
carboxyl-terminal sequence due to a T to C mutation at the first letter of
the termination codon of C57BL AhR. Two variants with reduced and
intermediate ligand binding activity were also found in human AhRs with
amino acid alterations equivalent to those of the DBA AhR. Importance of
the amino acid at position 381 of human AhR (equivalent to position 375 of
mouse AhR) in the ligand binding was confirmed by the fact that the
mutation of Val381 to Asp completely abolished the ligand binding activity
of human AhR.
Dioxin binding activities of polymorphic forms of mouse and human arylhydrocarbon receptors
Department of Chemistry, Faculty of Science, Tohoku University, Sendai, Japan.
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