Chaperone function of Hsp90-associated proteins
Chaperone function of Hsp90-associated proteins
复制标题
DOI：
10.1126/science.274.5293.1715
复制
发表时间：
1996-12-06
期刊：
影响因子：
56.9
通讯作者：
Buchner, J
中科院分区：
文献类型：
--
作者：
Bose, S;Weikl, T;Buchner, J
真核细胞的热休克蛋白90调节参与信号转导途径的蛋白质的活性，并且通常可以指导细胞内蛋白质折叠。热休克蛋白90执行至少一部分的功能，在一个复杂的一组特定的伴侣蛋白，包括脯氨酰异构酶家族的成员。Hsp90复合物的主要组分的性质通过使用体外蛋白质折叠测定进行了检查。其中两种成分FKBP 52和p23作为机制上不同的分子伴侣发挥作用。这些结果表明，在真核细胞的胞质溶胶中存在一个超级分子伴侣复合物。
The Hsp90 heat shock protein of eukaryotic cells regulates the activity of proteins involved in signal transduction pathways and may direct intracellular protein folding in general. Hsp90 performs at least part of its function in a complex with a specific set of partner proteins that include members of the prolyl isomerase family. The properties of the major components of the Hsp90 complex were examined through the use of in vitro protein folding assays. Two of the components, FKBP52 and p23, functioned as mechanistically distinct molecular chaperones. These results suggest the existence of a super-chaperone complex in the cytosol of eukaryotic cells.