Unspecific DNA binding of the DNA binding domain of the glucocorticoid receptor studied with flow linear dichroism

Per Hagmar; Karin Dahlman; Masayuki Takahashi; Jan Carlstedt-Duke; Jan Åke Gustafsson; Bengt Nordén

doi:10.1016/0014-5793(89)80922-6

Unspecific DNA binding of the DNA binding domain of the glucocorticoid receptor studied with flow linear dichroism

Per Hagmar, Karin Dahlman, Masayuki Takahashi, Jan Carlstedt-Duke, Jan Åke Gustafsson, Bengt Nordén

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	28-32
Number of pages	5
Journal	FEBS Letters
Volume	253
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(89)80922-6
State	Published - Aug 14 1989

Keywords

DNA-protein interaction
Glucocorticoid receptor
Linear dichroism

ASJC Scopus subject areas

Molecular Biology
Biophysics
Biochemistry

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10.1016/0014-5793(89)80922-6

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title = "Unspecific DNA binding of the DNA binding domain of the glucocorticoid receptor studied with flow linear dichroism",

abstract = "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.",

keywords = "DNA-protein interaction, Glucocorticoid receptor, Linear dichroism",

author = "Per Hagmar and Karin Dahlman and Masayuki Takahashi and Jan Carlstedt-Duke and Gustafsson, {Jan {\AA}ke} and Bengt Nord{\'e}n",

note = "Funding Information: Acknowledgements: This work is supported by the Swedish Natural Science Research Council and the Swedish Medical Research Council.",

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T1 - Unspecific DNA binding of the DNA binding domain of the glucocorticoid receptor studied with flow linear dichroism

AU - Hagmar, Per

AU - Dahlman, Karin

AU - Takahashi, Masayuki

AU - Carlstedt-Duke, Jan

AU - Gustafsson, Jan Åke

AU - Nordén, Bengt

N1 - Funding Information: Acknowledgements: This work is supported by the Swedish Natural Science Research Council and the Swedish Medical Research Council.

PY - 1989/8/14

Y1 - 1989/8/14

N2 - 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.

AB - 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.

KW - DNA-protein interaction

KW - Glucocorticoid receptor

KW - Linear dichroism

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Unspecific DNA binding of the DNA binding domain of the glucocorticoid receptor studied with flow linear dichroism

Abstract

Keywords

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