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J Biol Chem, Vol. 273, Issue 39, 25466-25471, September 25, 1998
From HSP Research Institute, Kyoto Research Park, Shimogyo-ku,
Kyoto 600-8813, Japan
Transcriptional induction of the
hsp70 gene is mediated by heat shock factor 1 (HSF1)
rapidly activated upon heat and other stresses. HSF2 has been thought
to be responsible for accumulation of HSP70 during hemin-induced
differentiation of human K562 erythroleukemia cells because of
accompanying acquisition of HSF2 DNA binding activity. However, there
has not been any direct evidence for such a functional role of HSF2.
The purpose of this study is to clarify the roles of HSF1 and HSF2 in
HSP70 induction in hemin-treated K562 cells. We show here that a
chimeric polypeptide of HSF2 and GAL4 DNA binding domain
(GAL4-BD-HSF2) was unable to induce a GAL4 binding site-containing
luciferase reporter gene in response to hemin and that exogenously
overproduced HSF2 also failed to increase expression of a heat shock
element-containing reporter. On the contrary, expression of a
GAL4-BD-HSF1 chimeric protein responded to hemin treatment as well as
to heat shock, and transiently overexpressed HSF1 caused
hemin-responsive induction of the reporter gene in a
dose-dependent manner. These results indicate that HSF1, rather than HSF2, primarily mediates the hemin-induced transcription of
the hsp70 gene.
Heat Shock Factor 1 Mediates Hemin-induced hsp70 Gene
Transcription in K562 Erythroleukemia Cells
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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