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J. Biol. Chem., Vol. 265, Issue 35, 21397-21400, Dec, 1990
LC Scherrer, FC Dalman, E Massa, S Meshinchi and WB Pratt
Untransformed steroid receptors in cytosol preparations are associated with
the 90-kDa heat shock protein hsp90, but the study of how hsp90 affects
receptor function has been held back by the inability to reassociate
steroid receptors with hsp90 in cell-free systems. Recently we showed
(Dalman, F.C., Bresnick, E. H., Patel, P. D., Perdew, G. H., Watson, S. J.,
and Pratt, W. B. (1989) J. Biol. Chem. 264, 19815-19821) that
glucocorticoid receptors translated in rabbit reticulocyte lysate bind to
hsp90 at the termination of receptor translation. In this work we show that
rabbit reticulocyte lysate promotes the temperature- dependent association
of hsp90 with immunopurified mouse L cell glucocorticoid receptors.
Reticulocyte lysate also promotes the temperature-dependent dissociation of
hormone-free receptors from a prebound receptor-DNA complex. The
glucocorticoid receptor is released from DNA in association with rabbit
hsp90, and reconstitution of the receptor-hsp90 complex is accompanied by
complete restitution of steroid binding activity and repression of DNA
binding activity. This is the first time that transformation of a DNA-bound
steroid receptor has been reversed and it raises the question of whether
the same or a similar system is involved in the termination of
transcriptional activation when steroid dissociates from DNA-bound
receptors in intact cells.
Structural and functional reconstitution of the glucocorticoid receptor- hsp90 complex
Department of Pharmacology, University of Michigan Medical School, Ann Arbor 48109.
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