The response to heat stress in six yeast species isolated from Antarct
ica was examined. The yeast were classified into two groups: one psych
rophilic, with a maximum growth temperature of 20 degrees C, and the o
ther psychrotrophic, capable of growth at temperatures above 20 degree
s C. In addition to species-specific heat shock prote in (hsp) profile
s, a heat shock (15 degrees C-25 degrees C for 3 h) induced the synthe
sis of a 110-kDa protein common to the psychrophiles, Mrakia stokesii,
M. frigida, and M. gelida, but not evident in Leucosporidium antarcti
cum. Immunoblot analyses revealed heat shock inducible proteins (hsps)
corresponding to hsps 70 and 90. Interestingly, no proteins correspon
ding to hsps 60 and 104 were observed in any of the psychrophilic spec
ies examined. In the psychrotrophic yeast, Leucosporidium fellii and L
. scottii, in addition to the presence of hsps 70 and 90, a protein co
rresponding to hsp 104 was observed. In psychrotrophic yeast, as obser
ved in psychrophilic yeast, the absence of a protein corresponding to
hsp 60 was noted. Relatively high endogenous levels of trehalose which
were elevated upon a heat shock were exhibited by all species. A 10 C
elsius degree increase in temperature above the growth temperature (15
degrees C) of psychrophiles and psychrotrophs was optimal for heat sh
ock induced thermotolerance. On the other hand, in psychrotrophic yeas
t grown at 25 degrees C, only a 5 Celsius degree increase in temperatu
re was necessary for heat shock induced thermotolerance. Induced therm
otolerance in all yeast species was coincident with hsp synthesis and
trehalose accumulation. It was concluded that psychrophilic and psychr
otrophic yeast, although exhibiting a stress response similar to mesop
hilic Saccharomyces cerevisiae, nevertheless had distinctive stress pr
otein profiles.