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J. Biol. Chem., Vol. 277, Issue 14, 11802-11810, April 5, 2002
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Gene through Physical Interaction with the
Nuclear Factor of Interleukin 6*
,
§,
From the Heat shock factor (HSF) 1 is the major heat shock
transcription factor that regulates stress-inducible synthesis of heat
shock proteins and is also essential in protection against endotoxic shock. Following our previous study, which demonstrated the
transcriptional repression of the IL-1
Department of Radiation Oncology, Dana
Farber Cancer Institute, Harvard Medical School and the
¶ Department of Radiation Oncology and the § Department
of Medicine, Molecular and Cell Biology Laboratory, Beth Israel and
Deaconess Medical Center, Harvard Medical School,
Boston, Massachusetts 02115
gene by HSF1
(Cahill, C. M., Waterman, W. R., Xie, Y., Auron, P. E.,
and Calderwood, S. K. (1996) J. Biol. Chem. 271, 24874-24879), we have examined the mechanisms of
transcriptional repression. Our studies show that HSF1 represses the
lipopolyliposaccharide-induced transcription of the
IL-1
promoter through direct interaction with the
nuclear factor of interleukin 6 (NF-IL6, also known as
CCAAT enhancer binding
protein (C/EBP
), an essential regulator in
IL-1
transcription. We show for the first time that HSF1
binds directly to NF-IL6 in vivo and antagonizes its
activity. The HSF1/NF-IL6 interaction involves a sequence of HSF1
containing the trimerization and regulatory domains and the bZip region
of NF-IL6. HSF1 has little effect on IL-1
promoter
activity stimulated by the essential monocytic transcription factor
Spi.1 but is strongly inhibitory to transcriptional activation by
NF-IL6 and to the synergistic activation by NF-IL6 and Spi.1. Because
of its ability to bind to specific C/EBP elements in the promoters of
multiple genes and its ability to interact with other transcription
factors, NF-IL6 is involved in transcriptional regulation of a wide
range of genes. Interaction between HSF1 and NF-IL6 could thus be an
important mechanism in HSF1 regulation of general gene transcription
during endotoxin stress.
To whom correspondence should be addressed: Dana Farber Cancer
Inst. and Joint Center for Radiation Therapy, Harvard Medical School,
44 Binney St., Boston, MA 02115. Tel.: 617-632-3885; Fax: 617-632-4599; E-mail: stuart_calderwood@dfci.harvard.edu.
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