Pouchelet M, St-Pierre E, Bibor-Hardy V, Simard R
Exp Cell Res. 1983 Dec;149(2):451-9. doi: 10.1016/0014-4827(83)90357-9.
The exposure of exponentially growing BHK cells to supranormal temperatures (41-44 degrees C, for 15 min to 1 h) induces the synthesis of a new set of proteins, the heat shock proteins, while the synthesis of proteins made before heat shock is repressed at 43 degrees C. Among the two major heat shock proteins induced, of molecular weight 70 K and 68 K, only the 70 kD protein is found bound to the nuclear matrix. This protein is resolved differently from the normal matrix proteins by isoelectric focusing and, when blotted, does not react with antibodies directed against nuclear matrices. These results show that the 70 kD heat shock protein is a new protein transferred from the cytoplasm to the nucleus, where it binds to the nuclear matrix, suggesting a structural role for this protein.
将指数生长的BHK细胞暴露于超常温度(41-44摄氏度,持续15分钟至1小时)会诱导合成一组新的蛋白质,即热休克蛋白,而在43摄氏度时,热休克前合成的蛋白质的合成会受到抑制。在诱导产生的两种主要热休克蛋白中,分子量分别为70K和68K,只有70kD的蛋白质与核基质结合。通过等电聚焦,这种蛋白质与正常基质蛋白的分离方式不同,并且在印迹时,它不与针对核基质的抗体发生反应。这些结果表明,70kD热休克蛋白是一种从细胞质转移到细胞核的新蛋白质,它在细胞核中与核基质结合,表明该蛋白质具有结构作用。