The immunoelectron microscopic analysis of Hsp104 under the hydrostatic pressure conditions

Hsp104 is one of the heat-shock proteins in the yeast Saccharomyces cerevisiae, and it works as a molecular chaperone. The chaperone function of Hsp depended on the temperature under hydrostatic pressure conditions. When yeast cells were exposed to mild heat of 43degreesC, the intracellular aggregates were appeared throughout the cells and induced Hsp104 to surround the aggregates. With immunoelectron microscopy, we observed that these cells moved under hydrostatic pressure. Under 100MPa hydrostatic pressure for 80min, Hsp104 dissappeared from intracellular aggregates at 35degreesC. However, on exposure to 100MPa at 4degreesC, the intracellular localization of Hsp104 did not change when compared to only mildly heatshockd cells. From these results, it suggests that Hsp104 works as a molecular chaperone under hydrostatic pressure at 35degreesC, but not 4degreesC.