Effect of temperature on the role of Hsp104 and trehalose in barotolerance of Saccharomyces cerevisiae.
We have studied the effect of temperature on the contribution of Hsp104 and trehalose to barotolerance using mutants deficient in Hsp104 and trehalose synthesis. When compared with a corresponding wild type strain, mutants of Hsp104 did not show temperature dependent barotolerance when the incubation temperature during the hydrostatic pressure treatment was increased. However, a mutant deficient in trehalose synthesis showed features similar to a wild type strain. Furthermore, the Hsp104 level was low in the insoluble fraction of the wild type strain after pressure treatment at 35 degrees C but not at 4 degrees C, and the protein profiles in the insoluble fraction were different between 35 degrees C and 4 degrees C. In contrast to the Hsp104 deficient mutants, the protein profile of the wild type after pressure treatment at 35 degrees C favors the role of Hsp104 as a disaggregator of proteins during hydrostatic pressure stress. These results suggest that the role of Hsp104 in barotolerance is temperature dependent in contrast to trehalose.
Iwahashi
H
H
National Institute of Bioscience and Human Technology, Tsukuba, Ibaraki, Japan. iwahashi@nibh.go.jp
Obuchi
K
K
Fujii
S
S
Komatsu
Y
Y
D000222:Adaptation, Physiological / Q000502:physiology*; D015180:Electrophoresis, Gel, Two-Dimensional; D006360:Heat-Shock Proteins / Q000502:physiology*; D011312:Pressure; D012441:Saccharomyces cerevisiae / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins; D013696:Temperature; D014199:Trehalose / Q000502:physiology*
D006360:Heat-Shock Proteins; D029701:Saccharomyces cerevisiae Proteins; C070972:HsP104 protein, S cerevisiae; D014199:Trehalose