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Complex modes of heat shock factor activation.

机译：热激因子激活的复杂模式。

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摘要

Eucaryotic organisms respond to elevated environmental temperatures by rapidly activating the expression of heat shock genes. The transcriptional activation of heat shock genes is mediated by a conserved upstream regulatory sequence, the heat shock element (HSE). Using an HSE-binding assay, we show that a cellular factor present in a range of vertebrate species binds specifically to the HSE. This factor is presumably the transcriptional activator of heat shock genes, heat shock factor (HSF). In vertebrates, the binding of HSF to the HSE was induced when cells were subjected to heat shock at high temperatures, even in the absence of protein synthesis. Under mild heat shock conditions, HSF binding was induced to a lesser extent, but this induction required protein synthesis, suggesting that synthesis of HSF itself, or an activating factor, is necessary for response to heat shock at intermediate temperatures. The inducibility of HSF binding in higher eucaryotes is contrasted with constitutive HSF binding activity in fungi. It appears that despite conservation of the HSE in evolution, the means by which HSF is activated to bind DNA in higher and lower eucaryotes may have diverged.
机译：真核生物通过迅速激活热休克基因的表达来应对升高的环境温度。热休克基因的转录激活由保守的上游调节序列，即热休克元件（HSE）介导。使用HSE结合测定，我们表明存在于一系列脊椎动物中的细胞因子与HSE特异性结合。该因子可能是热休克基因的转录激活因子，即热休克因子（HSF）。在脊椎动物中，即使在没有蛋白质合成的情况下，在高温下对细胞进行热激，也会诱导HSF与HSE的结合。在温和的热激条件下，HSF结合的诱导程度较小，但这种诱导需要蛋白质合成，这表明HSF本身或活化因子的合成对于中温下对热激的响应是必需的。 HSF结合在高等真核生物中的诱导性与真菌中本构性HSF结合活性形成对比。似乎尽管进化中保护了HSE，但激活HSF结合高等和低等真核生物中DNA的方法可能有所不同。

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