Tetrameric structure of the nonactivated glucocorticoid receptor in cell extracts and intact cells

FEBS Lett. 1988 Dec 5;241(1-2):234-8. doi: 10.1016/0014-5793(88)81068-8.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Dimethyl Suberimidate
  • Electrophoresis, Polyacrylamide Gel
  • Lymphoma / metabolism
  • Macromolecular Substances
  • Mice
  • Molecular Weight
  • Protein Conformation
  • Receptors, Glucocorticoid / isolation & purification*
  • Receptors, Glucocorticoid / metabolism

Substances

  • Macromolecular Substances
  • Receptors, Glucocorticoid
  • Dimethyl Suberimidate