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This response is characterized by the induction of heat shock proteins (HSPs) and regulated mainly at the level of transcription by heat shock factor (HSF). Vertebrate cells possess four HSF genes, which are located in the conserved syntenic regions among species. The amino acid sequences of the DNA-binding domain (DBD) and oligomerization domain (HR-A/B) located in the N-terminal region are highly conserved. The DBD interacts with genomic DNA, and HR-A/B is required for the formation of an HSF trimer that binds to DNA with high affinity.

1997; Nakai and Morimoto 1993; Rabindran et al. 1991; Sarge et al. 1991; Schuetz et al. 1991), researchers have 42 R. Takii and M. Fujimoto investigated which HSF activates the HSP genes. Biochemical analyses showed that human and mouse HSF1, but not HSF2, acquires DNA-binding activity and translocated to the nucleus in response to heat shock, suggesting that HSF1 is involved in the induction of HSP genes (Baler et al. 1993; Sarge et al. 1993). Subsequently, disruption of HSF genes in mouse embryonic fibroblasts (MEFs) demonstrated that mouse HSF1 is required for the HSP induction during heat shock (McMillan et al.

Proc Natl Acad Sci U S A 89:1666–1670 Ungewickell E (1985) The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles. EMBO J 4:3385–3391 Vierke G, Engelmann A, Hebbeln C, Thomm M (2003) A novel archaeal transcriptional regulator of heat shock response. J Biol Chem 278:18–26 Wang G, Ying Z, Jin X, Tu N, Zhang Y, Phillips M, Moskophidis D, Mivechi NF (2004) Essential requirement for both hsf1 and hsf2 transcriptional activity in spermatogenesis and male fertility.

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