Fiorenza M T, Farkas T, Dissing M, Kolding D, Zimarino V
Department of Molecular Cell Biology, University of Copenhagen, Denmark.
Nucleic Acids Res. 1995 Feb 11;23(3):467-74. doi: 10.1093/nar/23.3.467.
A central step in the transcriptional activation of heat shock genes is the binding of the heat shock factor (HSF) to upstream heat shock elements (HSEs). In vertebrates, HSF1 mediates the ubiquitous response to stress stimuli, while the role of a second HSE-binding factor, HSF2, is still unclear. In this work we show that both factors are expressed in a wide range of murine tissues and each exists as two splicing isoforms. Although HSFs are virtually ubiquitous proteins, their abundance is predominant in testis and variable among other tissues, indicating specific regulations of their expression. A low level of DNA-binding activity of HSF1, detected in many tissues, is probably physiological and is not explained by an anomalous regulation of one of the two isoforms. Our observations suggest that these regulatory proteins may all have roles in fully developed tissues. This possibility is not mutually exclusive of a role of HSF2 during cellular differentiation and tissue development [L. Sistonen, K. D. Sarge and R. I. Morimoto (1994), Mol. Cell. Biol., 14, 2087-2099].
热休克基因转录激活的一个核心步骤是热休克因子（HSF）与上游热休克元件（HSE）的结合。在脊椎动物中，HSF1介导对应激刺激的普遍反应，而第二个HSE结合因子HSF2的作用仍不清楚。在这项研究中，我们表明这两种因子在多种小鼠组织中均有表达，且每种因子都以两种剪接异构体的形式存在。尽管HSF实际上是普遍存在的蛋白质，但它们在睾丸中的丰度最高，在其他组织中则有所不同，这表明它们的表达存在特定调控。在许多组织中检测到的HSF1的低水平DNA结合活性可能是生理性的，并非由两种异构体之一的异常调控所致。我们的观察结果表明，这些调节蛋白可能在完全发育的组织中都发挥作用。这种可能性与HSF2在细胞分化和组织发育过程中的作用并不相互排斥[L. Sistonen、K. D. Sarge和R. I. Morimoto（1994年），《分子与细胞生物学》，14，2087 - 2099]。
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