Petersen R, Lindquist S
Department of Molecular Genetics and Cell Biology, University of Chicago, IL 60637.
Gene. 1988 Dec 10;72(1-2):161-8. doi: 10.1016/0378-1119(88)90138-2.
When heat-shocked Drosophila cells are returned to normal temperatures, heat-shock protein (HSP) synthesis is repressed and normal protein synthesis is restored. The repression of HSP70 synthesis is accompanied by the selective degradation of its mRNA. We have engineered cells to produce a modified hsp70 mRNA that behaves exactly as the wild-type message. That is, it is stable during heat shock but degraded during recovery when protein synthesis returns to normal. When this message, placed under the control of the metallothionein promoter, is induced at normal temperatures it is rapidly degraded, with a half life of 15-30 min. Apparently, the hsp70 message is inherently unstable. During heat-shock, degradation of the message is suspended; during recovery degradation is restored.
当热休克果蝇细胞恢复到正常温度时，热休克蛋白（HSP）的合成受到抑制，正常蛋白质合成得以恢复。HSP70合成的抑制伴随着其mRNA的选择性降解。我们构建了能够产生一种修饰的hsp70 mRNA的细胞，这种mRNA的行为与野生型mRNA完全相同。也就是说，它在热休克期间是稳定的，但在蛋白质合成恢复正常的恢复过程中会被降解。当这个在金属硫蛋白启动子控制下的mRNA在正常温度下被诱导时，它会迅速降解，半衰期为15 - 30分钟。显然，hsp70 mRNA本质上是不稳定的。在热休克期间，mRNA的降解暂停；在恢复过程中，降解恢复。
