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J Biol Chem, Vol. 273, Issue 30, 18974-18978, July 24, 1998
From the Department of Biochemistry, Molecular Biology and Cell
Biology, Northwestern University, Evanston, Illinois 60208
The heat shock response is a highly conserved
mechanism that allows cells to withstand a variety of stress
conditions. Activation of this response is characterized by increased
synthesis of heat shock proteins (HSPs), which protect cellular
proteins from stress-induced denaturation. Heat shock transcription
factors (HSFs) are required for increased expression of HSPs during
stress conditions and can be found in complexes containing components
of the Hsp90 molecular chaperone machinery, raising the possibility
that Hsp90 is involved in regulation of the heat shock response. To
test this, we have assessed the effects of mutations that impair
activity of the Hsp90 machinery on heat shock related events in
Saccharomyces cerevisiae. Mutations that either reduce the
level of Hsp90 protein or eliminate Cpr7, a CyP-40-type cyclophilin
required for full Hsp90 function, resulted in increased
HSF-dependent activities. Genetic tests also revealed that
Hsp90 and Cpr7 function synergistically to repress gene expression from
HSF-dependent promoters. Conditional loss of Hsp90 activity
resulted in both increased HSF-dependent gene expression
and acquisition of a thermotolerant phenotype. Our results reveal that
Hsp90 and Cpr7 are required for negative regulation of the heat shock
response under both stress and nonstress conditions and establish a
specific endogenous role for the Hsp90 machinery in S. cerevisiae.
Requirement for Hsp90 and a CyP-40-type Cyclophilin in Negative
Regulation of the Heat Shock Response
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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