Protein-protein interactions between the DNA-binding domains of nuclear receptors: Influence on DNA-binding

Karin Dahlman-Wright, Kaj Grandien, Stefan Nilsson, Jan Åke Gustafsson, Jan Carlstedt-Duke

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

The glucocorticoid and thyroid hormone receptors have the capacity to bind as dimers to palindromic DNA-binding sites. Protein-protein interactions between the DNA-binding domains of glucocorticoid receptor dimers restrict the DNA-binding to elements where the half-sites are separated by three base pairs, whereas DNA-binding by the thyroid hormone receptor does not appear to require a strict half-site spacing. We have previously shown that a five amino-acid segment close the the C-terminal zinc-binding site (D-box) was involved in dimerization of the glucocorticoid receptor (GR) DNA-binding domain (Dahlman-Wright et al., 1991, J. Biol. Chem., 266, 3107-3112). Here we provide functional evidence, using mutated thyroid hormone receptor DNA-binding domains, that this five amino acid segment (D-box) of the GR interacts with the equivalent segment on the second DNA-binding domain in the dimer. In contrast, the thyroid hormone receptor DNA-binding domain binds to palindromic thyroid hormone response elements in a weakly co-operative manner, independent of the D-box.

Original languageEnglish (US)
Pages (from-to)239-250
Number of pages12
JournalJournal of Steroid Biochemistry and Molecular Biology
Volume45
Issue number4
DOIs
StatePublished - Apr 1993

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Endocrinology
  • Clinical Biochemistry
  • Cell Biology

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