Tanguay R M, Vincent M
Can J Biochem. 1982 Mar;60(3):306-15. doi: 10.1139/o82-037.
The intracellular distribution of cellular and heat shock induced proteins (hsp) was studied during a heat shock to Drosophila Kc cells. The different hsp's are unequally distributed between the intracellular organelles; while hsp 84 shows an exclusive cytoplasmic location, hsp 70 is equally distributed between the nucleus and the cytoplasm. The low molecular weight (MW) hsp's 22--26 are mainly concentrated in the nuclear fraction. Hsp 34 also shows a preferential nuclear localization but differs from the 22-26 hsp group with regard to its solubility in salt. During the heat shock (HS) treatment, a major preexisting microsomal polypeptide of relative mass (Mr) 45 000 with some properties similar to cytoskeletal proteins is translocated to the nuclear pellet. This translocation does not occur during arsenite treatment which also induces the synthesis of some hsp's. Furthermore, the hsp's synthesized in response to this arsenite treatment do not become associated with the nucleus as during the HS. Consequently the nuclear translocation of the 45 000 Mr protein does not seem to be involved in the induction of the high MW group of hsp's. Furthermore, it suggests that the hsp's which are found in the nuclear pellet upon HS do not have a nuclear localization per se. It rather reflects a temperature-dependent translocation of certain cellular proteins and hsp to the nucleus during a HS.
在对果蝇Kc细胞进行热休克处理期间，研究了细胞内蛋白质和热休克诱导蛋白（hsp）的细胞内分布。不同的热休克蛋白在细胞内细胞器之间分布不均；hsp 84仅位于细胞质中，而hsp 70在细胞核和细胞质中分布均匀。低分子量（MW）的热休克蛋白22 - 26主要集中在细胞核部分。hsp 34也主要定位于细胞核，但在盐中的溶解度与22 - 26热休克蛋白组不同。在热休克（HS）处理期间，一种相对分子质量（Mr）为45000且具有一些与细胞骨架蛋白相似特性的主要预先存在的微粒体多肽会转移到核沉淀中。在亚砷酸盐处理期间不会发生这种转移，亚砷酸盐处理也会诱导一些热休克蛋白的合成。此外，响应亚砷酸盐处理合成的热休克蛋白不会像在热休克期间那样与细胞核结合。因此，45000 Mr蛋白的核转移似乎与高分子量热休克蛋白组的诱导无关。此外，这表明在热休克后在核沉淀中发现的热休克蛋白本身并没有核定位。它更反映了在热休克期间某些细胞蛋白和热休克蛋白向细胞核的温度依赖性转移。
