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Tetrameric structure of the nonactivated glucocorticoid receptor in cell extracts and intact cells
Author(s) -
Rexin Martin,
Busch Willi,
Segnitz Bernd,
Gehring Ulrich
Publication year - 1988
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(88)81068-8
Subject(s) - tetramer , glucocorticoid receptor , protein subunit , receptor , glucocorticoid , chemistry , cell , biochemistry , microbiology and biotechnology , steroid , biology , hormone , enzyme , endocrinology , gene
Mouse lymphoma cells contain a nonactivated glucocorticoid receptor of M r ∼330000 which is heteromeric in nature and is unable to bind to DNA. Following affinity labeling of the steroid‐binding subunit and subsequent cross‐linking with dimethyl suberimidate at various times either in cell extracts or in intact cells, a series of labeled bands was detected in SDS gels. From the molecular masses of completely and partially cross‐linked complexes we conclude that the large nonactivated receptor is a tetramer composed of two 90 kDa subunits, one 50 kDa polypeptide and one steroid‐binding subunit.