Protein-protein interactions facilitate DNA binding by the glucocorticoid receptor DNA-binding domain

K. Dahlman-Wright, H. Siltala-Roos, J. Carlstedt-Duke, J. A. Gustafsson

Research output: Contribution to journalArticlepeer-review

94 Scopus citations

Abstract

We have studied the interaction of the DNA-binding domain of the glucocorticoid receptor with a glucocorticoid response element from the tyrosine aminotransferase gene. This response element consists of two binding sites (half-sites) for the glucocorticoid receptor DNA-binding domain. The sequences of these two half-sites are not identical, and we have previously shown that binding occurs preferentially to one of the half-sites (Tsai, S.-Y., Carlstedt-Duke, J., Weigel, N. L., Dahlman, K., Gustafsson, J.-Å., Tsai, M.-J., and O'Malley, B. W. (1988) Cell 55, 361-369). We show here that binding to the low affinity half-site is dependent on previous occupancy of the high affinity half-site. This facilitated binding is dependent on the distance between the two half-sites and their relative orientation but is not dependent on the integrity of the DNA backbone. This is consistent with a model where DNA binding is not only dependent on interactions between the protein and its DNA target sequence but is also influenced by interactions between the protein molecules bound.

Original languageEnglish (US)
Pages (from-to)14030-14035
Number of pages6
JournalJournal of Biological Chemistry
Volume265
Issue number23
StatePublished - 1990

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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