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J. Biol. Chem., Vol. 269, Issue 45, 27894-27899, 11, 1994
KA Hutchison, KD Dittmar and WB Pratt
The hormone-binding domain of the glucocorticoid receptor must be bound to
heat shock protein (hsp) 90 for it to have a high-affinity steroid binding
conformation. We have recently demonstrated that hsp70 is required for
cell-free assembly of the receptor.hsp90 complex and concomitant activation
of steroid binding activity (Hutchison, K.A., Dittmar, K.D., Czar, M.J.,
and Pratt, W. B. (1994) J. Biol. Chem. 269, 5043-5049). hsp90 and hsp70 are
known to exist together in a cytosolic complex containing several other
proteins, and in this work we ask if all of the factors required for proper
receptor folding and heterocomplex assembly are preassociated in this
multiprotein complex. The multiprotein complex was immunoadsorbed to
protein A-agarose from rabbit reticulocyte lysate using the 3G3 monoclonal
IgM directed against hsp90. When this immunopellet is mixed with
immunadsorbed mouse glucocorticoid receptor and incubated at 30 degrees C
with ATP/Mg2+ and KCl, the receptor is converted to the steroid binding
conformation. When the immunoadsorbed multiprotein hsp90 complex is washed
extensively, it loses a weakly bound protein (not hsp70 or hsp90) that is
required for receptor activation. This protein factor is contained in a
Centricon C-100 filtrate of lysate which reconstitutes the receptor
activating activity of the washed hsp90 complex. The hsp90 complex can be
released from the 3G3 antibody, and in the presence of the protein factor
in the Centricon C-100 filtrate it converts the receptor into a functional
heterocomplex with hsp90. The results support the proposal that the various
components of reticulocyte lysate that are required to refold the
glucocorticoid receptor to the steroid binding state are preassociated with
each other, acting as a self- sufficient protein folding machine.
All of the factors required for assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90 are preassociated in a self-sufficient protein folding structure, a "foldosome"
Department of Pharmacology, University of Michigan Medical School, Ann Arbor 48109.
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