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Molecular and Cellular Biology, August 2003, p. 5882-5895, Vol. 23, No. 16
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.16.5882-5895.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Activation of Heat Shock Genes Is Not Necessary for Protection by Heat Shock Transcription Factor 1 against Cell Death Due to a Single Exposure to High Temperatures

Sachiye Inouye,1 Kensaku Katsuki,1,2 Hanae Izu,1 Mitsuaki Fujimoto,1 Kazuma Sugahara,1 Shu-ichi Yamada,3 Yoichi Shinkai,3 Yoshitomo Oka,2,{dagger} Yumiko Katoh,1 and Akira Nakai1*

Department of Biochemistry and Molecular Biology,1 Third Department of Internal Medicine, Yamaguchi University School of Medicine, Ube 755-8505,2 Department of Cell Biology, Institute for Virus Research, Kyoto University, Kyoto 606-8507, Japan3

Received 24 March 2003/ Returned for modification 8 May 2003/ Accepted 20 May 2003

Heat shock response, which is characterized by the induction of a set of heat shock proteins, is essential for induced thermotolerance and is regulated by heat shock transcription factors (HSFs). Curiously, HSF1 is essential for heat shock response in mammals, whereas in avian HSF3, an avian-specific factor is required for the burst activation of heat shock genes. Amino acid sequences of chicken HSF1 are highly conserved with human HSF1, but those of HSF3 diverge significantly. Here, we demonstrated that chicken HSF1 lost the ability to activate heat shock genes through the amino-terminal domain containing an alanine-rich sequence and a DNA-binding domain. Surprisingly, chicken and human HSF1 but not HSF3 possess a novel function that protects against a single exposure to mild heat shock, which is not mediated through the activation of heat shock genes. Overexpression of HSF1 mutants that could not bind to DNA did not restore the susceptibility to cell death in HSF1-null cells, suggesting that the new protective role of HSF1 is mediated through regulation of unknown target genes other than heat shock genes. These results uncover a novel role of vertebrate HSF1, which has been masked underthe roles of heat shock proteins.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, Yamaguchi University School of Medicine, Minami-Kogushi 1-1-1, Ube 755-8505, Japan. Phone: 81 836 22 2214. Fax: 81 836 22 2315. E-mail: anakai{at}yamaguchi-u.ac.jp.

{dagger} Present address: Molecular Metabolism and Diabetes, Internal Medicine, Tohoku University, Tohoku, Japan.

Molecular and Cellular Biology, August 2003, p. 5882-5895, Vol. 23, No. 16
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.16.5882-5895.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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