Muñoz A, Alonso M A, Carrasco L
Virology. 1984 Aug;137(1):150-9. doi: 10.1016/0042-6822(84)90018-7.
Incubation of HeLa cells at supraoptimal temperatures induces the synthesis of a class of proteins known as heat-shock or stress-response proteins. After restoration of cells to physiological temperatures heat-shock protein synthesis continues for several hours. Normal cellular translation eventually recovers even if cells are treated with actinomycin D, indicating that neither normal cellular mRNAs nor components of the translation machinery are irreversibly modified by heat treatment. The synthesis of heat-shock proteins after poliovirus infection is more resistant to inhibition than normal host proteins. Nevertheless, their synthesis is also inhibited in infected cells, even in cells treated with human interferon under which conditions viral RNA replication and viral translation are blocked. Translation of heat-shock proteins is also resistant to hypertonic shock indicating that their mRNAs bind ribosomes with high affinity.
在超适温度下培养HeLa细胞会诱导一类被称为热休克或应激反应蛋白的蛋白质合成。将细胞恢复到生理温度后，热休克蛋白的合成会持续数小时。即使细胞用放线菌素D处理，正常的细胞翻译最终也会恢复，这表明热处理既不会不可逆地修饰正常细胞的mRNA，也不会修饰翻译机制的组成部分。脊髓灰质炎病毒感染后热休克蛋白的合成比正常宿主蛋白更能抵抗抑制作用。然而，它们的合成在受感染的细胞中也会受到抑制，即使在用人干扰素处理的细胞中也是如此，在这种条件下病毒RNA复制和病毒翻译会被阻断。热休克蛋白的翻译也能抵抗高渗休克，这表明它们的mRNA以高亲和力结合核糖体。
