TRANSCRIPTIONAL AND TRANSLATIONAL REGULATION OF MAJOR HEAT-SHOCK PROTEINS AND PATTERNS OF TREHALOSE MOBILIZATION DURING HYPERTHERMIC RECOVERY IN REPRESSED AND DEREPRESSED SACCHAROMYCES-CEREVISIAE
C. Gross et K. Watson, TRANSCRIPTIONAL AND TRANSLATIONAL REGULATION OF MAJOR HEAT-SHOCK PROTEINS AND PATTERNS OF TREHALOSE MOBILIZATION DURING HYPERTHERMIC RECOVERY IN REPRESSED AND DEREPRESSED SACCHAROMYCES-CEREVISIAE, Canadian journal of microbiology, 44(4), 1998, pp. 341-350
Patterns of heat shock gene transcription and translation, as well as
trehalose content, were investigated in both glucose (repressed) and a
cetate (derepressed) grown cells of Saccharomyces cerevisiae during he
at shock and subsequent return of cells to 25 degrees C. Heat-shocked
cells (37 degrees C for 30 min), grown in either glucose- or acetate-s
upplemented media, initially acquired high thermotolerance to a 50 deg
rees C heat stress, which was progressively lost when cultures were al
lowed to recover at 25 degrees C and subsequently exposed to a second
heat stress. In all cases, with the notable exception of repressed cel
ls of a relatively thermosensitive strain, inhibition of protein synth
esis and coincident decrease in trehalose accumulation during the heat
shock had little effect on the kinetics of loss of thermotolerance. H
ear shock at 37 degrees C elicited a marked increase in transcription
and translation of genes encoding major heat shock proteins (hsps). Du
ring recovery at 25 degrees C, both metabolic activities were suppress
ed followed by a gradual increase in hsp mRNA transcription to levels
observed prior to heat shock. De novo translation of hsp mRNAs, howeve
r, was no longer observed during the recovery phase, although immunode
tection analyses demonstrated persistence of high levels of hsps 104,
90, 70, and 60 in cells throughout the 240-min recovery period. In add
ition, while heat shock induced trehalose was rapidly degraded during
recovery in repressed cells, levels remained high in derepressed cells
. Results therefore indicated that the progressive loss of induced the
rmotolerance exhibited by glucose- and acetate-grown cells was not clo
sely correlated with levels of hsp or trehalose. It was concluded that
both constitutive and de novo synthesized hsps require heat shock ass
ociated activation to confer thermotolerance and this modification is
progressively reversed upon release from the heat-shocked state.