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J. Biol. Chem., Vol. 265, Issue 7, 3615-3618, Mar, 1990
FC Dalman, RJ Koenig, GH Perdew, E Massa and WB Pratt
We have recently reported that the glucocorticoid receptor (GR) becomes
bound to the 90-kDa heat shock protein (hsp90) at or near the end of
receptor translation in vitro (Dalman, F. C., Bresnick, E. H., Patel, P.
D., Perdew, G. H., Watson, S. J., Jr., and Pratt, W. B. (1989) J. Biol.
Chem. 264, 19815-19821). In this paper we compare the hsp90 binding and DNA
binding activities of the thyroid hormone receptor (TR) to those of the GR
after cell-free translation of the two receptors in rabbit reticulocyte
lysate. In contrast to the newly translated GR, which is bound to hsp90 and
must be transformed to the DNA binding state, the TR is not bound to hsp90
and is translated in its DNA binding form without any requirement for
transformation. When the GR is translated in wheat germ extract, which does
not contain hsp90, it is translated in its DNA binding form in the same
manner as the TR synthesized in reticulocyte lysate. These observations
provide direct evidence that binding of GR to hsp90 is associated with
repression of its DNA binding function. The fact that the TR does not bind
to hsp90 and is translated in its DNA binding form is consistent with the
different behavior of this receptor with respect to classic steroid
receptors in the intact cell. We propose that binding to hsp90 may account
for the fact that most of the steroid receptors are recovered in the
cytosolic fraction after lysis of hormone-free cells in low salt buffer
whereas the hormone-free TR is recovered in tight association with the
nucleus.
In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90
Department of Pharmacology, University of Michigan Medical School, Ann Arbor 48109.
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