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J Biol Chem, Vol. 274, Issue 3, 1472-1478, January 15, 1999
From the Department of Pharmacology, The University of Michigan
Medical School, Ann Arbor, Michigan 48109
It is established that the multiprotein heat
shock protein 90 (hsp90)-based chaperone system acts on the ligand
binding domain of the glucocorticoid receptor (GR) to form a GR·hsp90
heterocomplex and to convert the receptor ligand binding domain to the
steroid-binding state. Treatment of cells with the hsp90 inhibitor
geldanamycin inactivates steroid binding activity and increases the
rate of GR turnover. We show here that a portion of neuronal
nitric-oxide synthase (nNOS) exists as a molybdate-stabilized
nNOS·hsp90 heterocomplex in the cytosolic fraction of human embryonic
kidney 293 cells stably transfected with rat nNOS. Treatment of human
embryonic kidney 293 cells with geldanamycin both decreases nNOS
catalytic activity and increases the rate of nNOS turnover. Similarly,
geldanamycin treatment of nNOS-expressing Sf9 cells partially
inhibits nNOS activation by exogenous heme. Like the GR, purified
heme-free apo-nNOS is activated by the DE52-retained fraction of rabbit reticulocyte lysate, which also assembles nNOS·hsp90 heterocomplexes. However, in contrast to the GR, heterocomplex assembly with hsp90 is
not required for increased heme binding and nNOS activation in this
cell-free system. We propose that, in vivo, where access by
free heme is limited, the complete hsp90-based chaperone machinery is
required for sustained opening of the heme binding cleft and nNOS
activation, but in the heme-containing cell-free nNOS-activating system
transient opening of the heme binding cleft without hsp90 is sufficient
to facilitate heme binding.
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