Abstract：
:Heat shock and other proteotoxic stresses cause accumulation of nonnative proteins that trigger activation of heat shock protein (Hsp) genes. A chaperone/Hsp functioning as repressor of heat shock transcription factor (HSF) could make activation of hsp genes dependent on protein unfolding. In a novel in vitro system, in which human HSF1 can be activated by nonnative protein, heat, and geldanamycin, addition of Hsp90 inhibits activation. Reduction of the level of Hsp90 but not of Hsp/c70, Hop, Hip, p23, CyP40, or Hsp40 dramatically activates HSF1. In vivo, geldanamycin activates HSF1 under conditions in which it is an Hsp90-specific reagent. Hsp90-containing HSF1 complex is present in the unstressed cell and dissociates during stress. We conclude that Hsp90, by itself and/or associated with multichaperone complexes, is a major repressor of HSF1.
journal_name
Celljournal_title
Cellauthors
Zou J,Guo Y,Guettouche T,Smith DF,Voellmy Rdoi
10.1016/s0092-8674(00)81588-3subject
Has Abstractpub_date
1998-08-21 00:00:00pages
471-80issue
4eissn
0092-8674issn
1097-4172pii
S0092-8674(00)81588-3journal_volume
94pub_type
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