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Originally published In Press as doi:10.1074/jbc.M109296200 on January 18, 2002

J. Biol. Chem., Vol. 277, Issue 14, 11802-11810, April 5, 2002
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Heat Shock Factor 1 Represses Transcription of the IL-1beta Gene through Physical Interaction with the Nuclear Factor of Interleukin 6*

Yue XieDagger , Changmin ChenDagger §, Mary Ann Stevenson, Philip E. Auron§, and Stuart K. CalderwoodDagger ||

From the Dagger  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

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-1beta 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-1beta promoter through direct interaction with the nuclear factor of interleukin 6 (NF-IL6, also known as CCAAT enhancer binding protein (C/EBPbeta ), an essential regulator in IL-1beta 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-1beta 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.

* This work was supported by National Institutes of Health Grants CA47407, CA31303, and CA50642 (to S. K. C.) and CA68544 (to P. E. A.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| 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.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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