FIGURE 3: Hsp42-SPGs colocalize with heat shock-induced misfolded protein. (A) Heat shock-induced misfolded protein colocalizes to Hsp42-SPGs. Three-day stationary phase cells carrying Hsp42-BFP (Red) and an unstable mutant form of GFP-tagged luciferase (Green) were imaged before (28°C) and after (42°C) 30 min of mild heat shock at 42°C. The percentages of Hsp42-SPG-positive cells that colocalized with luciferase dots increased from 16 ± 2% to 70 ± 4% after heat shock. (B) Heat shock-induced protein aggregates are cleared more efficiently in Q cells. The luciferase-containing cells were monitored under a time-lapse microscope initiated before heat shock (see Materials and Methods). The numbers of cells containing heat shock-induced protein aggregates were counted immediately after heat shock (0 min) or after recovering at 28°C for 90 min (90 min). 48% of luciferase aggregates ([85 – 44]/85 = 48%) were cleared in Q cells, but only 17% ([58 – 48]/58 = 17%) were cleared in NQ cells. Three samples were analyzed in each condition and at least 100 cells were counted in each sample.