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Interaction of the Mr = 90,000 heat shock protein with the steroid-binding domain of the glucocorticoid receptor


Interaction of the Mr = 90,000 heat shock protein with the steroid-binding domain of the glucocorticoid receptor



Journal of Biological Chemistry 263(34): 18520-18523



ISSN/ISBN: 0021-9258

PMID: 3192546

We have investigated the physiochemical characteristics of trypsin-treated, molybdate-stabilized glucocorticoid-receptor complexes from rat liver in the presence of 10 mM sodium molybdate by high performance ion-exchange chromatography, high performance size-exclusion chromatography, and sedimentation analysis. Trypsin treatment was performed under conditions previously reported to degrade the monomeric Mr approximately 94,000 steroid-binding protein to an Mr approximately 27,000 ligand-binding entity (Wrange, O., and Gustafsson, J.-A. (1978) J. Biol. Chem. 253, 856-865). Also in the presence of molybdate, an Mr approximately 27,000 steroid-binding fragment was obtained by limited trypsinization. However, no major differences in the tested physicochemical parameters were seen when trypsin-treated glucocorticoid-receptor complexes were compared with crude cytosolic complexes. Furthermore, the Mr approximately 27,000 steroid-binding fragment generated in the presence of molybdate could be immunoprecipitated by antibodies specific for the glucocorticoid receptor-associated Mr approximately 90,000 heat shock protein. These results provide direct evidence for an interaction of the Mr approximately 90,000 heat shock protein with the steroid-binding domain of the glucocorticoid receptor, known to correspond to the C-terminal third of the receptor protein.

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Accession: 017967622

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Related references

Interaction of the m r equals 90000 heat shock protein with the steroid binding domain of the glucocorticoid receptor. Journal of Biological Chemistry 263(34): 18520-18523, 1988

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