Banerji S S, Berg L, Morimoto R I
J Biol Chem. 1986 Nov 25;261(33):15740-5.
Transient incubation of chicken lymphoblastoid (MSB) cells at elevated temperatures induces the synthesis of three heat shock proteins of 89,000 Da (HSP89), 70,000 Da (HSP70), and 23,000 Da (HSP23). We have examined the effects of heat shock on the transcription and post-transcriptional regulation of the chicken HSP70 and beta-actin genes. The rate of HSP70 transcription is rapidly induced by heat shock, reaches maximal levels by 60 min, and thereafter decreases. The level of HSP70 mRNA increases 20-fold by 60 min and remains constant through 6 h of heat shock. Upon return of heat-shocked cells to normal growth temperatures, the level of HSP70 mRNA rapidly decreases to pre-heat shock levels. These results suggest that HSP70 mRNA is stably maintained and translated during heat shock, but rapidly degraded during recovery from heat shock. The effect of heat shock on beta-actin mRNA is opposite to the apparent stabilizing effects of elevated temperatures on HSP70 mRNA.
鸡淋巴母细胞样（MSB）细胞在高温下短暂孵育会诱导合成三种热休克蛋白，分别为89,000道尔顿（HSP89）、70,000道尔顿（HSP70）和23,000道尔顿（HSP23）。我们研究了热休克对鸡HSP70和β-肌动蛋白基因转录及转录后调控的影响。热休克迅速诱导HSP70转录速率，60分钟时达到最高水平，此后下降。HSP70 mRNA水平在60分钟时增加20倍，并在热休克6小时内保持恒定。热休克细胞恢复到正常生长温度后，HSP70 mRNA水平迅速降至热休克前水平。这些结果表明，HSP70 mRNA在热休克期间稳定维持并进行翻译，但在从热休克恢复过程中迅速降解。热休克对β-肌动蛋白mRNA的影响与高温对HSP70 mRNA的明显稳定作用相反。
