Beaulieu J F, Tanguay R M
Ontogénèse et Génétique Moléculaires, Centre Hospitalier Université Laval, Sainte-Foy, Québec, Canada.
Eur J Biochem. 1988 Mar 1;172(2):341-7. doi: 10.1111/j.1432-1033.1988.tb13892.x.
In Drosophila, the hsp 70 family consists of a group of proteins of similar molecular masses (hsps 68, 70 and 72) that exist as multiple isoforms. In this report, it is shown that hsps 68, 70 and 72 from Drosophila cells can be purified by affinity chromatography on ATP-agarose. Furthermore it is demonstrated that the multiple members of the hsp 70 family, which accumulate in large amounts in the nucleus during a heat shock, can be specifically solubilized from the isolated nuclei fraction by ATP. One of the major cognate proteins (hsc 70) also shows similar behavior. These data suggest that most, if not all, of the related Drosophila hsps 70 possess, like their mammalian counterparts, an ATP-binding site which could be related to their function in the stress response.
在果蝇中，热休克蛋白70（hsp 70）家族由一组分子量相似的蛋白质（hsps 68、70和72）组成，这些蛋白质以多种同工型存在。在本报告中，结果表明，果蝇细胞中的hsps 68、70和72可通过ATP-琼脂糖亲和层析进行纯化。此外还证明，在热休克期间大量积累在细胞核中的hsp 70家族的多个成员，可通过ATP从分离的细胞核部分中特异性溶解。其中一种主要的同源蛋白（hsc 70）也表现出类似的行为。这些数据表明，大多数（如果不是全部的话）相关的果蝇hsps 70，与其哺乳动物对应物一样，具有一个ATP结合位点，这可能与其在应激反应中的功能有关。
