Regulation of Hsp70 function by a eukaryotic DnaJ homolog.
Regulation of Hsp70 function by a eukaryotic DnaJ homolog.
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DOI：
10.1016/s0021-9258(19)36777-8
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发表时间：
1992-10
期刊：
影响因子：
--
通讯作者：
D. Cyr;Xiangyang Lu;M. Douglas
中科院分区：
文献类型：
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作者：
D. Cyr;Xiangyang Lu;M. Douglas
我们报告，从酿酒酵母，Hsp 70 SSA 1，纯化的细胞质Hsp 70同源物，表现出弱的ATP酶活性，这是由一个纯化的真核生物dnaJp同源物（YDJ 1 p）的刺激。通过天然凝胶电泳分析Hsp 70 SSA 1和永久未折叠蛋白羧甲基化α-乳白蛋白（CMLA）之间稳定复合物的形成。Hsp 70 SSA 1与CMLA的亲和力似乎受YDJ 1 p的调节。仅在YDJ 1 p和ATP存在下观察到CMLA-Hsp 70 SSA 1复合物形成和预先结合至Hsp 70 SSA 1的CMLA的释放的显著减少。因此，在真核细胞中，Hsp 70 SSA 1和YDJ 1 p在执行Hsp 70 SSA 1分子伴侣活性中功能性地相互作用。
We report that a purified cytoplasmic Hsp70 homolog from Saccharomyces cerevisiae, Hsp70SSA1, exhibits a weak ATPase activity, which is stimulated by a purified eukaryotic dnaJp homolog (YDJ1p). Stable complex formation between Hsp70SSA1 and the permanently unfolded protein carboxymethylated alpha-lactalbumin (CMLA) was assayed by native gel electrophoresis. The affinity of Hsp70SSA1 for CMLA appeared to be regulated by YDJ1p. Significant reduction in both CMLA-Hsp70SSA1 complex formation and the release of CMLA pre-bound to Hsp70SSA1 was observed only in the presence of both YDJ1p and ATP. Thus, Hsp70SSA1 and YDJ1p interact functionally in the execution of Hsp70SSA1 chaperone activities in the eukaryotic cell.