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Cdc37 associates with the heatshock protein 90(Hsp90) molecular chaperone as one of several auxiliary proteins that arecollectively referred to as Hsp90 cochaperones. Cdc37 has been proposed to be aspecificity factor for Hsp90, directing it notably towards kinases. It is notknown whether Cdc37 is essential for viability in the budding yeastSaccharomyces cerevisiae because of Hsp90-dependent or independent functions orboth. Sti1 and Cpr7 are nonessential Hsp90 cochaperones that bind to a commonsurface on Hsp90 through tetratricopeptide repeats (TPR). We have found thatSti1 is specifically retained from yeast extracts by immobilized Cdc37.Similarly, the endogenous proteins are also found in a complex. Moreover,purified recombinant Sti1 and Cdc37 interact in the complete absence of Hsp90.Complexes between Cdc37 and Sti1 are not unique to this TPR protein sinceendogenous Cdc37 can be copurified with exogenously expressed Cpr7 fused toglutathioneStransferase. The heterogeneity of Cdc37 complexes, both with andwithout Hsp90, may expand the functional diversity of Cdc37. Here we show thatthe combination of cdc37 and sti1 mutations is synthetically lethal, suggestingthat direct contacts between Cdc37 and Sti1 may at least contribute to vitalfunctions in yeast.

The Hsp90 Co-Chaperones Cdc37 and Sti1 Interact Physically and Genetically