Protein-DNA interactions at a dioxin-responsive enhancer: Evidence that the transformed Ah receptor is heteromeric

Cornelis Elferink, Thomas A. Gasiewicz, James P. Whitlock

Research output: Contribution to journalArticle

92 Citations (Scopus)

Abstract

The Ah receptor in rat hepatic cytosol was transformed to a DNA-binding form by incubation in vitro with the ligand 2,3,7,8-tetrachlorodibenzo-p-dioxin. The transformed receptor was covalently cross-linked to a bromodeoxyuridine-substituted DNA recognition motif by exposure to ultraviolet irradiation. Analyses of the cross-linked protein-DNA complexes by gel electrophoresis and autoradiography imply that the DNA-binding form of the liganded Ah receptor is composed of two protein components, whose molecular masses are about 110 and 100 kDa. Protease digestion studies suggest that the two components have different primary structures. Photoaffinity labeling studies imply that the smaller protein is the ligand-binding component of the receptor. These findings constitute biochemical evidence that the DNA-binding form of the Ah receptor is a heterodimer.

Original languageEnglish (US)
Pages (from-to)20708-20712
Number of pages5
JournalJournal of Biological Chemistry
Volume265
Issue number33
StatePublished - Nov 25 1990
Externally publishedYes

Fingerprint

Dioxins
DNA
Proteins
Ligands
Nucleotide Motifs
Bromodeoxyuridine
Autoradiography
Cytosol
Electrophoresis
Molecular mass
Digestion
Peptide Hydrolases
Gels
Labeling
Rats
Irradiation
Liver

ASJC Scopus subject areas

  • Biochemistry

Cite this

Protein-DNA interactions at a dioxin-responsive enhancer : Evidence that the transformed Ah receptor is heteromeric. / Elferink, Cornelis; Gasiewicz, Thomas A.; Whitlock, James P.

In: Journal of Biological Chemistry, Vol. 265, No. 33, 25.11.1990, p. 20708-20712.

Research output: Contribution to journalArticle

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