Title: Interaction of androgen response elements with the DNA-binding domain of the rat androgen receptor expressed in Escherichia coli
Authors: De Vos, Piet ×
Claessens, Frank
Winderickx, Joris
Van Dijck, Patrick
Celis, Linda
Peeters, Benjamin
Rombauts, Wilfried
Heyns, Walter
Verhoeven, Guido #
Issue Date: Feb-1991
Series Title: Journal of Biological Chemistry vol:266 issue:6 pages:3439-3443
Abstract: A fragment of the rat androgen receptor (amino acids 533-637) containing the DNA-binding domain was produced in Escherichia coli as a fusion product with protein A of Staphylococcus aureus. The fusion protein was purified on IgG-Sepharose, a method that does not involve the use of denaturing agents. Approximately 4 mg of fusion protein was obtained from 500 ml of bacterial culture. In gel shift assays, the recombinant DNA-binding domain displays an affinity for a fragment of the long terminal repeat of mouse mammary tumor virus and for an intronic fragment of the gene coding for the C3 component of the androgen-regulated rat prostatic binding protein. In a DNase I footprinting assay, the fusion protein protects a sequence in the C3 fragment that has previously been shown to act as a functional androgen response element. Interestingly, a single base pair mutation in the response element, which abolishes androgen inducibility, also destroys the ability to interact with the recombinant androgen receptor DNA-binding domain.
ISSN: 0021-9258
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Clinical and Experimental Endocrinology
Molecular Physiology of Plants and Micro-organisms Section - miscellaneous
Biochemistry Section (Medicine) (-)
Molecular Microbiology and Biotechnology Section - miscellaneous
Laboratory of Molecular Endocrinology
× corresponding author
# (joint) last author

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