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. Author manuscript; available in PMC: 2011 Feb 12.
Published in final edited form as: Mol Cell. 2010 Feb 12;37(3):333–343. doi: 10.1016/j.molcel.2010.01.005

Figure 6. Co-chaperone binding to non-phosphorylatable Hsp90 mutants.

Figure 6

A) & B) yHsp90-His6 from wt or swe1Δ yeast and yHsp90His6-Y24F were precipitated and their interaction with co-chaperones was detected by immunoblotting.

C & D) COS7 cells were transfected with indicated FLAG-Hsp90 constructs (empty vector pcDNA3 [c], FLAG-hHsp90α [wt], or FLAG-hHsp90α-Y38F [Y38F]). FLAG-Hsp90 was immunoprecipitated and associated Aha1, p23, p60Hop and p50Cdc37 were detected by immunoblotting.