Journal: Cell Stress & Chaperones

Article Title: Comparative analysis of the impact of Heat shock protein 90 kDa or Cdc37 mutation on the yeast proteome

doi: 10.1016/j.cstres.2026.100164

Figure Lengend Snippet: (a) Simplified model of the Hsp90 folding pathway. Client (dark gray oval) bound to a chaperone such as Cdc37 (light gray diamond) is targeted to the open conformation of Hsp90 (gray). After ATP binds, Hsp90 shifts to the closed conformation. ATP hydrolysis is associated with a return to the open conformation. The Hsc82-G309S and Cdc37-S14A mutants target early steps in the pathway associated with client loading (1, loading). The Hsc82-Q380K mutant targets reopening (2), and the G424D mutant targets an unknown step in the pathway (other). (b) Growth of yeast strains after 2 days at the indicated temperature on YPD media. ATP, adenosine triphosphate; YPD, yeast extract peptone dextrone.

Article Snippet: Yeast were transformed by lithium acetate methods and were grown in either yeast extract peptone dextrone (YPD) (1% Bacto yeast extract, 2% peptone, and 2% dextrose) or defined synthetic complete media supplemented with 2% dextrose.

Techniques: Mutagenesis