中文摘要：

热吃惊 factor-DNA 相互作用为在优核质理解导致压力的基因表示的规章的机制是批评的。在这研究，我们分析了在里面到目标基因 ScSSA1， ScSSA4， HSP30 和 HSP104 的倡导者的酵母热吃惊因素(HSF ) 的 vivo 绑定，用染色质免疫降水。以前的工作建议酵母 HSF 根本 DNA 组成地一定温度。HSF 目标基因的表示在 post-transcriptional 水平被调整。然而，我们的结果显示 HSF 不在正常温度(23 度 C ) 绑在 ScSSA4 和 HSP30 的倡导者。到这些倡导者的绑定被热应力很快在 39 度 C 导致。HSF 在非压力条件下面绑在 ScSSA1 和 HSP104 倡导者，但是在底层。热应力很快在 HSF 的绑定导致著名增加到这二基因。与目标基因的表示好的 HSF 倡导者有约束力的相互关联的水平的动力学，建议 HSF 的表示指向基因是至少部分 HSF 倡导者有约束力的稳定性的结果和随后的抄写刺激。

英文摘要：

Heat shock factor-DNA interaction is critical for understanding the regulatory mechanisms of stress-induced gene expression in eukaryotes. In this study, we analyzed the in vivo binding of yeast heat shock factor （HSF） to the promoters of target genes ScSSA1, ScSSA4, HSP30 and HSP104, using chromatin immunoprecipitation. Previous work suggested that yeast HSF is constitutively bound to DNA at all temperatures. Expression of HSF target genes is regulated at the post-transcriptional level. However, our results indicated that HSF does not bind to the promoters of ScSSA4 and HSP30 at normal temperature （23 ℃）. Binding to these promoters is rapidly induced by heat stress at 39 ℃. HSF binds to ScSSA1 and HSP104 promoters under non-stress conditions, but at a low level. Heat stress rapidly leads to a notable increase in the binding of HSF to these two genes. The kinetics of the level of HSF-promoter binding correlate well with the expression of target genes, suggesting that the expression of HSF target genes is at least partially the result of HSF-promoter binding stability and subsequent transcription stimulation.