Structure and function of the dioxin receptor: A DNA-binding protein similar to steroid hormone receptors

Lorenz Poellinger, Anna Wilhelmsson, Scott Cuthill, Johan Lund, Peter Söderkvist, Mikael Gillner, Jan Åke Gustafsson

Research output: Contribution to journalArticle

Abstract

In analogy to steroid hormone receptors, the rat hepatic dioxin receptor binds to bulk DNA and heparin in vitro. The affinity of the dioxin receptor for both DNA and heparin is dependent on the binding of ligand and is negatively affected by the presence of sodium molybdate in the homogenization buffer. Limited proteolysis of the dioxin receptor with trypsin which is known to eliminate the DNA-binding property of the glucocorticoid receptor also resulted in a loss of DNA-binding activity and a decreased strength in the interaction with heparin of the in vitro liganded dioxin receptor. However, limited proteolysis with trypsin did not result in any change in gross structural properties of the dioxin receptor. These data suggest that the DNA-binding activity of the dioxin receptor resides within a discrete and relatively small functional domain of the protein.

Original languageEnglish (US)
Pages (from-to)1681-1686
Number of pages6
JournalChemosphere
Volume16
Issue number8-9
DOIs
StatePublished - 1987

ASJC Scopus subject areas

  • Environmental Engineering
  • Environmental Chemistry
  • Chemistry(all)
  • Pollution
  • Health, Toxicology and Mutagenesis

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