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J. Biol. Chem., Vol. 267, Issue 20, 13952-13957, Jul, 1992
KA Hutchison, LF Stancato, R Jove and WB Pratt
In a recent study demonstrating the cell-free reconstitution of the
pp60v-src-hsp90 complex, we found that the tyrosine kinase-hsp90 complex is
stabilized by molybdate (Hutchison, K. A., Brott, B. K., De Leon, J. H.,
Perdew, G. H., Jove, R., and Pratt, W. B. (1992) J. Biol. Chem. 267,
2902-2908). In this paper, we examine in detail the stabilization of this
protein-protein interaction by transition metal oxyanions. The
pp60v-src-hsp90 complex is stabilized by sodium molybdate with the same
concentration dependence as the glucocorticoid receptor-hsp90 complex. As
with the steroid receptor heterocomplexes, vanadate and tungstate also
stabilize the pp60v-src-hsp90 interaction. Passage of cytosol through a
Chelex-100 metal-chelating resin destabilizes the native pp60v-src-hsp90
complex, suggesting that the complex is normally stabilized by an
endogenous metal factor. Readdition of either the heat-stable components of
cytosol or a partially purified endogenous metal factor stabilizes the
metal- depleted complex. Molybdate also stabilizes the presence of p50, a
known hsp90-associated protein, in the pp60v-src heterocomplex. Given the
identical effects of transition metal oxyanions on both pp60v-src- and
steroid receptor-hsp90 complexes and the lack of any sequence homology
between pp60v-src and the receptors, it seems very likely that it is the
common component, hsp90, that contains the site of the metal interaction.
The protein-protein complex between pp60v-src and hsp90 is stabilized by molybdate, vanadate, tungstate, and an endogenous cytosolic metal
Department of Pharmacology, University of Michigan Medical School, Ann Arbor 48109.
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