Tetrameric structure of the nonactivated glucocorticoid receptor in cell extracts and intact cells.
Mouse lymphoma cells contain a nonactivated glucocorticoid receptor of Mr approximately 330,000 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.
Rexin
M
M
Institut für Biologische Chemie, Universität, Heidelberg, FRG.
Busch
W
W
Segnitz
B
B
Gehring
U
U
D000818:Animals; D002460:Cell Line; D004120:Dimethyl Suberimidate; D004591:Electrophoresis, Polyacrylamide Gel; D008223:Lymphoma / Q000378:metabolism; D046911:Macromolecular Substances; D051379:Mice; D008970:Molecular Weight; D011487:Protein Conformation; D011965:Receptors, Glucocorticoid / Q000302:isolation & purification* / Q000378:metabolism
D046911:Macromolecular Substances; D011965:Receptors, Glucocorticoid; D004120:Dimethyl Suberimidate