Unspecific DNA binding of the DNA binding domain of the glucocorticoid receptor studied with flow linear dichroism.
The unspecific interaction between the DNA-binding domain of the human glucocorticoid receptor and DNA was studied using linear dichroism (LD) and circular dichroism (CD) spectroscopy. The amplitude of the LD signal was found to increase upon addition of protein at ionic strengths less than 60 nM Na+, indicating an increased persistence length of the complex compared to uncomplexed DNA. Analysis of the LD spectrum suggests that the binding does not involve intercalation of tyrosine residues. Evidence of saturation is found at a binding stoichiometry of approximately 5 DNA base pairs per protein monomer.
Department of Physical Chemistry, Chalmers University of Technology, S-412 Gothenburg, Sweden.
P
P
Hagmar
K
K
Dahlman
M
M
Takahashi
J
J
Carstedt-Duke
J
J
Gustafsson
B
B
Nordén
D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D066298:In Vitro Techniques; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D011965:Receptors, Glucocorticoid / Q000378:metabolism* / Q000648:ultrastructure; D013057:Spectrum Analysis
D004268:DNA-Binding Proteins; D011965:Receptors, Glucocorticoid; D004247:DNA