分子伴侣Hsp90在26S蛋白酶体的组装和维持中发挥作用。
The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome.
作者信息
Imai Jun, Maruya Mikako, Yashiroda Hideki, Yahara Ichiro, Tanaka Keiji
机构信息
Department of Molecular Oncology and Department of Cell Biology, Tokyo Metropolitan Institute of Medical Science, Honkomagome 3-18-22, Bunkyo-ku, Tokyo 113-8613, CREST, Japan.
出版信息
EMBO J. 2003 Jul 15;22(14):3557-67. doi: 10.1093/emboj/cdg349.
Abstract
Hsp90 has a diverse array of cellular roles including protein folding, stress response and signal transduction. Herein we report a novel function for Hsp90 in the ATP-dependent assembly of the 26S proteasome. Functional loss of Hsp90 using a temperature-sensitive mutant in yeast caused dissociation of the 26S proteasome. Conversely, these dissociated constituents reassembled in Hsp90-dependent fashion both in vivo and in vitro; the process required ATP-hydrolysis and was suppressed by the Hsp90 inhibitor geldanamycin. We also found genetic interactions between Hsp90 and several proteasomal Rpn (Regulatory particle non-ATPase subunit) genes, emphasizing the importance of Hsp90 to the integrity of the 26S proteasome. Our results indicate that Hsp90 interacts with the 26S proteasome and plays a principal role in the assembly and maintenance of the 26S proteasome.
摘要
热休克蛋白90（Hsp90）在细胞中具有多种作用，包括蛋白质折叠、应激反应和信号转导。在此，我们报道了Hsp90在26S蛋白酶体的ATP依赖性组装中的新功能。利用酵母中的温度敏感突变体使Hsp90功能丧失，导致26S蛋白酶体解离。相反，这些解离的成分在体内和体外都以依赖Hsp90的方式重新组装；该过程需要ATP水解，并且被Hsp90抑制剂格尔德霉素抑制。我们还发现Hsp90与几个蛋白酶体Rpn（调节颗粒非ATP酶亚基）基因之间存在遗传相互作用，强调了Hsp90对26S蛋白酶体完整性的重要性。我们的结果表明，Hsp90与26S蛋白酶体相互作用，并在26S蛋白酶体的组装和维持中起主要作用。
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