Tanguay R M, Camato R, Lettre F, Vincent M
Can J Biochem Cell Biol. 1983 Jun;61(6):414-20. doi: 10.1139/o83-056.
In Drosophila Kc cultured cell lines, heat shock induces an increased synthesis of one of the core histones, H2B. This is accompanied by a reduction in the rate of synthesis of H1 and the other core histones, suggesting a noncoordinated expression of histones during heat shock. Arsenite which has a heat-shock mimicking effect does not induce an increase in the synthesis of H2B. The increased expression of H2B during heat shock shows a temperature dependency similar to that of the low molecular weight heat-shock proteins being observed at temperatures higher than 33 degrees C. A full heat-shock response is observed after a short 15-min shock at 37 degrees C, suggesting a rapid transcriptional response of the H2B gene and possibly a decreased transcription of the other histones and (or) an accelerated decay of their corresponding mRNAs. This increased synthesis of H2B seems under transcriptional control since it can be inhibited, like the other major heat-shock proteins, by the addition of actinomycin D.
在果蝇Kc培养细胞系中,热休克诱导核心组蛋白之一H2B的合成增加。这伴随着H1和其他核心组蛋白合成速率的降低,表明热休克期间组蛋白的表达不协调。具有热休克模拟效应的亚砷酸盐不会诱导H2B合成增加。热休克期间H2B表达的增加表现出与在高于33摄氏度的温度下观察到的低分子量热休克蛋白相似的温度依赖性。在37摄氏度下短暂15分钟的休克后观察到完全的热休克反应,表明H2B基因有快速的转录反应,并且可能其他组蛋白的转录减少和(或)其相应mRNA的加速降解。H2B这种合成增加似乎受转录控制,因为与其他主要热休克蛋白一样,添加放线菌素D可抑制其合成。