Brissette J L, Russel M, Weiner L, Model P
Rockefeller University, New York, NY 10021.
Proc Natl Acad Sci U S A. 1990 Feb;87(3):862-6. doi: 10.1073/pnas.87.3.862.
Filamentous phage infection induces the synthesis of large amounts of an Escherichia coli protein, phage shock protein (Psp), the product of a previously undescribed gene. This induction is due to the phage gene IV protein, pIV, an integral membrane protein. The uninduced level of Psp is undetectable, but when induced by prolonged synthesis of pIV, it can become one of the most abundant proteins in the cell. Psp is also synthesized transiently in response to several stresses (heat, ethanol, and osmotic shock). High-level synthesis occurs only after extreme treatment. Unlike the members of the heat shock regulon, Psp induction does not require the heat shock sigma factor, sigma 32; some stimuli that elicit sigma 32-dependent heat shock proteins do not induce Psp synthesis. The level of Psp induction after extreme stress is even higher in sigma 32 mutant cells, which are unable to mount a normal heat shock response, suggesting that these parallel stress responses are interrelated.
丝状噬菌体感染会诱导大肠杆菌大量合成一种蛋白质——噬菌体休克蛋白（Psp），它是一个此前未被描述的基因的产物。这种诱导作用是由噬菌体基因IV蛋白pIV引起的，pIV是一种整合膜蛋白。未诱导时，Psp的水平检测不到，但当通过长时间合成pIV进行诱导时，它会成为细胞中含量最丰富的蛋白质之一。Psp也会在应对几种应激（热、乙醇和渗透压休克）时短暂合成。只有在极端处理后才会发生高水平合成。与热休克调节子的成员不同，Psp的诱导不需要热休克σ因子σ32；一些引发依赖σ32的热休克蛋白的刺激不会诱导Psp合成。在无法产生正常热休克反应的σ32突变细胞中，极端应激后Psp的诱导水平甚至更高，这表明这些平行的应激反应是相互关联的。
