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Unspecific DNA binding of the DNA binding domain of the glucocorticoid receptor studied with flow linear dichroism
Author(s) -
Hagmar Per,
Dahlman Karin,
Takahashi Masayuki,
Carlstedt-Duke Jan,
Gustafsson Jan-Åke,
Nordén Bengt
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80922-6
Subject(s) - linear dichroism , circular dichroism , dna , chemistry , intercalation (chemistry) , glucocorticoid receptor , ionic strength , dna binding domain , biophysics , crystallography , hmg box , monomer , base pair , biochemistry , dna binding protein , receptor , biology , inorganic chemistry , transcription factor , organic chemistry , aqueous solution , gene , polymer
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.