Heat shock factor-1 and the heat shock cognate 70 protein associate in high molecular weight complexes in the cytoplasm of NIH-3T3 cells.
Heat shock factor-1 and the heat shock cognate 70 protein associate in high molecular weight complexes in the cytoplasm of NIH-3T3 cells.
复制标题
热休克因子 1 和热休克同源 70 蛋白在 NIH-3T3 细胞细胞质中的高分子量复合物中结合。
DOI：
10.1006/bbrc.1995.2090
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发表时间：
1995
影响因子：
3.1
通讯作者：
Calderwood,SK
中科院分区：
文献类型：
--
作者：
Nunes,SL;Calderwood,SK
在NIH 3 T3细胞中研究了热休克转录因子1（HSF-1）与70 kD热休克同源蛋白（HSC 70）的相互作用。发现HSF-1在非应激细胞的细胞质中与HSC 70以大（Mr 400- 500，000）复合物相关联。热休克后，HSF-1在细胞核中浓缩成更小、更稳定的复合物，不含HSC 70，这表明复合物内发生了显著的重排。这些实验表明，在核定位过程中，热休克对HSF-1复合物的结构和稳定性产生了深远的影响，并支持HSC 70结合可能控制HSF-1功能的假设。
Interaction of heat shock transcription factor-1 (HSF-1) with the seventy kilodalton heat shock cognate protein (HSC70) was examined in NIH 3T3 cells. HSF-1 was found in the cytoplasm of non-stressed cells associated with HSC70 in large (Mr 400-500,000) complexes. After heat shock, HSF-1 became concentrated in the nucleus in smaller, more stable complexes that did not contain HSC70, an indication of significant rearrangement within the complexes. These experiments show a profound effect of heat shock on the structure and stability of HSF-1 complexes during nuclear localization and support the hypothesis that HSC70 binding may control HSF-1 function.