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

Karin Dahlman-Wright, Helmi Siltala-Roos, Jan Carlstedt-Duke, Jan Åke Gustafsson

    Research output: Contribution to journalArticlepeer-review

    107 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 - Aug 15 1990

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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