Nunes S L, Calderwood S K
Dana Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.
Biochem Biophys Res Commun. 1995 Aug 4;213(1):1-6. doi: 10.1006/bbrc.1995.2090.
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.
在NIH 3T3细胞中检测了热休克转录因子1（HSF-1）与70千道尔顿热休克同源蛋白（HSC70）的相互作用。在未受应激的细胞胞质中发现HSF-1与HSC70以大的（分子量400 - 500,000）复合物形式存在。热休克后，HSF-1在细胞核中聚集形成较小、更稳定且不含HSC70的复合物，这表明复合物内部发生了显著重排。这些实验表明热休克对HSF-1复合物在核定位过程中的结构和稳定性有深远影响，并支持HSC70结合可能控制HSF-1功能这一假说。
