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Vol. 12, No. 5, pp. 654-666, March 1, 1998
1 Department of Biochemistry, Molecular Biology, and Cell
Biology, Rice Institute for Biomedical Research, Northwestern
University, Evanston, Illinois 60208 USA;
2 Biotechnology
Research Institute, National Research Council, Montreal, Canada
The rapid yet transient transcriptional activation of heat shock
genes is mediated by the reversible conversion of HSF1 from an inert
negatively regulated monomer to a transcriptionally active DNA-binding
trimer. During attenuation of the heat shock response, transcription of
heat shock genes returns to basal levels and HSF1 reverts to an inert
monomer. These events coincide with elevated levels of Hsp70 and other
heat shock proteins (molecular chaperones). Here, we show that the
molecular chaperone Hsp70 and the cochaperone Hdj1 interact directly
with the transactivation domain of HSF1 and repress heat shock gene
transcription. Overexpression of either chaperone represses the
transcriptional activity of a transfected GAL4-HSF1 activation domain
fusion protein and endogenous HSF1. As neither the activation of HSF1
DNA binding nor inducible phosphorylation of HSF1 was affected, the
primary autoregulatory role of Hsp70 is to negatively regulate HSF1
transcriptional activity. These results reveal that the repression of
heat shock gene transcription, which occurs during attenuation, is due
to the association of Hsp70 with the HSF1 transactivation domain, thus
providing a plausible explanation for the role of molecular chaperones
in at least one key step in the autoregulation of the heat shock response.
[Key Words: Transcriptional control; autoregulation; heat shock proteins; Hsp70; activation domain]
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