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J Biol Chem, Vol. 274, Issue 7, 4133-4139, February 12, 1999

Heat-induced Oligomerization of the Molecular Chaperone Hsp90
INHIBITION BY ATP AND GELDANAMYCIN AND ACTIVATION BY TRANSITION METAL OXYANIONS

Ahmed Chadli, Moncef M. Ladjimi^¶, Etienne-Emile Baulieu, and Maria Grazia Catelli

From the  INSERM, U 488, Neurosteroïdes et Système Nerveux, 80 rue du Général Leclerc, 94276 Le Krémlin Bicêtre, the ^¶ Laboratoire de Biochimie des Signaux Régulateurs Cellulaires et Moléculaires, CNRS, UMR-7631, 96 Boulevard Raspail, 75006 Paris, and the  Laboratoire d'Endocrinologie, Métabolisme et Développement, CNRS, UPR-1524, CHU Cochin Port Royal, 24 rue du Faubourg St. Jacques, 75014 Paris, France

It has been previously reported that heat shock protein 90 (Hsp90) oligomerizes at high temperatures and displays concomitantly a novel chaperone activity (Yonehara, M., Minami, Y., Kawata, Y., Nagai, J., and Yahara, I. (1996) J. Biol. Chem., 271, 2641-2645). In order to better define these oligomerization properties at high temperatures and to know whether they are influenced by modulators of Hsp90 function, heat-induced oligomerization of highly purified dimeric Hsp90 has been investigated over a wide range of temperature and protein concentrations by native polyacrylamide gel electrophoresis and size exclusion chromatography. Whereas below 50 °C, the dimeric form is maintained over a large range of concentrations, at the critical temperature of 50 °C, a sharp transition from dimeric to higher order oligomeric species takes place within minutes, in a highly ordered process, suggesting that a conformational change, leading to the appearance of a new oligomerization site, occurs in Hsp90 dimer. Moreover, at and above the critical temperature, the extent of oligomerization increases with Hsp90 concentration.

Formation of high order oligomers at high temperatures is sensitive to modulators of Hsp90 function. ATP and geldanamycin, both known to bind to the same pocket of Hsp90, are inhibitors of this process, whereas molybdate, vanadate, and Nonidet P-40, which are thought to increase surface hydrophobicity of the protein, are activators. Thus, oligomerization of Hsp90 at high temperatures may be mediated through hydrophobic interactions that are hindered by ligands and favored by transition metal oxyanions.

The fact that the heat-induced oligomerization of Hsp90 is affected by specific ligands that modulate its properties also suggests that this process may be involved in cell protection during heat shock.

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