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J. Biol. Chem., Vol. 266, Issue 6, 3482-3490, Feb, 1991
FC Dalman, LC Scherrer, LP Taylor, H Akil and WB Pratt
In this work, we used two approaches to localize the 90-kDa heat shock
protein (hsp90)-binding site within the hormone-binding domain of the
glucocorticoid receptor. In the first approach, derivatives of the
glucocorticoid receptor deleted for increasing portions of the COOH
terminus were translated in rabbit reticulocyte lysate, and the
[35S]methionine-labeled translation products were immunoadsorbed with the
8D3 monoclonal antibody against hsp90. The data suggest that a segment from
amino acids 604 to 659 (mouse) of the receptor is required for hsp90
binding. We have recently shown that the internal deletion mutant of the
mouse receptor (delta 574-632) binds hsp90, although the complex is
somewhat unstable (Housley, P. R., Sanchez, E. R., Danielsen, M., Ringold,
G. M., and Pratt, W. B. (1990) J. Biol. Chem. 265, 12778-12781). The two
observations indicate that amino acids 574- 659 are involved in forming a
stable receptor-hsp90 complex and that region 632-659 is especially
important. To test this hypothesis directly, we synthesized three peptides
corresponding to segments in region 624-665 and three peptides spanning the
highly conserved sequence at amino acids 582-617, and we then tested the
ability of the peptides to compete for the association of hsp90 with the L
cell glucocorticoid receptor. In this assay, the immunopurified hsp90-free
mouse receptor is incubated with rabbit reticulocyte lysate, which directs
the association of rabbit hsp90 with the mouse receptor, simultaneously
converting the receptor to the steroid binding state. All three peptides
spanning region 624-665 and a peptide corresponding to segment 587-606
inhibited both hsp90 association with the receptor and reconstitution of
steroid binding capacity. The data from all of the approaches support a
two-site model for the hsp90-binding site in which the critical contact
site occurs in region 632-659, which contains a short proline-containing
hydrophobic segment and adjacent dipole-plus-cysteine motif that are
conserved among all of the hsp90- binding receptors in the superfamily. A
second hsp90 contact site is predicted in region 574-632, which contains
the only highly conserved amino acid sequence in the receptor superfamily
outside of the DNA- binding domain.
Localization of the 90-kDa heat shock protein-binding site within the hormone-binding domain of the glucocorticoid receptor by peptide competition
Department of Pharmacology, University of Michigan Medical School, Ann Arbor 48109-0626.
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