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Papers In Press, published online ahead of print January 18, 2002
Radiation Oncology, Dana Farber Cancer Institute, Boston, MA 02115
Corresponding Author: yue_xie{at}dfci.harvard.edu
Heat shock factor (HSF) 1 is the major heat shock transcription factor that regulates stress inducible synthesis of heat shock proteins (HSPs) and is also essential in protection against endotoxic shock. Following our previous study, which demonstrated the transcriptional repression of the interleukin (IL)-1 beta gene by HSF1 (1), we have examined the mechanisms of transcriptional repression. Our studies show that HSF1 represses the LPS-induced transcription of the IL-1 beta promoter through direct interaction with NF-IL6 (C/EBPß), an essential regulator in IL-1 beta 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 beta 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.
J. Biol. Chem, 10.1074/jbc.M109296200
Submitted on September 26, 2001
Revised on January 18, 2002
Accepted on January 17, 2002
Heat shock factor-1 (HSF1) represses transcription of the interleukin 1 beta (IL-1 beta) gene through physical interaction with nuclear factor of interleukin-6 (NF-IL6)
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