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Domains of the human androgen receptor and glucocorticoid receptor involved in binding to the nuclear matrix
Author(s) -
van Steensel Bas,
Jenster Guido,
Damm Klaus,
Brinkmann Albert O.,
van Driel Roel
Publication year - 1995
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240570312
Subject(s) - nuclear matrix , nuclear receptor , glucocorticoid receptor , nuclear receptor co repressor 1 , nuclear receptor coactivator 1 , scaffold/matrix attachment region , androgen receptor , receptor , matrix (chemical analysis) , dna binding domain , microbiology and biotechnology , pelp 1 , binding domain , estrogen related receptor gamma , chromatin , biology , chemistry , binding site , biochemistry , dna , genetics , transcription factor , chromatin remodeling , gene , prostate cancer , cancer , chromatography
Steroid receptors have been reported to bind to the nuclear matrix. The nuclear matrix is operationally defined as the residual nuclear structure that remains after extraction of most of the chromatin and all soluble and loosely bound componnets. To obtain insight in the molecular mechanism of the interaction of steroid receptors with the nuclear matrix, we studied the binding of several deletion mutants of the human androgen receptor (hAR) and the human glucocorticoid receptor (hGR) to the nuclear matrix. Receptor binding was tested for two different nuclear matrix preparations: complete matrices, in which most matrix proteins are retained during the isolation procedure, and depleted matrices, which consist of only a subset of these proteins. The results show that the C‐terminal domain of the hAR binds tightly to both depleted and complete matrices. In addition, at least one other domain of the hAR binds to complete matrices but not to depleted matrices. In contrast to the hAR, the hGR binds only to complete matrices. For this interaction both the DNA‐binding domain and the C‐terminal domain of the hGR are required, whereas the N‐terminal domain is not. We conclude that specific protein domains of the hAR and the hGR are involved in binding to the nuclear matrix. In addition, our results indicate that the hAR and the hGR are attached to the nuclear matrix through different molecular interactions.