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Ectopic BH3-only protein Bim acts as a cochaperone to positively regulate Hsp70 in yeast
The Journal of Biochemistry ( IF 2.1 ) Pub Date : 2021-06-28 , DOI: 10.1093/jb/mvab073
Hao Pan 1 , Ting Song 1 , Ziqian Wang 1 , Yafei Guo 2 , Hong Zhang 2 , Tong Ji 1 , Keke Cao 1 , Zhichao Zhang 1
Affiliation  

The chaperone heat shock protein 70 (Hsp70) is conserved from bacteria to humans and is crucial for avoiding protein misfolding under stress. Bim functions, mainly as one of the B-cell lymphoma 2 (Bcl-2) family proapoptotic members, were identified to be a cochaperone of Hsp70. Herein, we reported that ectopic Bim could constitute the interactions with intrinsic Hsp70 and translate its positive cochaperone activity in vitro to the yeast growth promotion and help Hsp70 to fold its client Ras-like protein. With the help of a specific Hsp70/Bim disruptor, we illustrated that Hsp70/Bim dimers rescue yeast from heat shock. In an organism lacks apoptotic Bcl-2 factors, the proapoptotic Bim in mammalian cells exhibits prosurvival functions.

中文翻译:

仅异位 BH3 蛋白 Bim 作为辅助伴侣在酵母中正向调节 Hsp70

伴侣热休克蛋白 70 (Hsp70) 从细菌到人类是保守的,对于避免蛋白质在压力下错误折叠至关重要。Bim 功能,主要作为 B 细胞淋巴瘤 2 (Bcl-2) 家族的促凋亡成员之一,被确定为 Hsp70 的共同伴侣。在此,我们报道了异位 Bim 可以与内在 Hsp70 形成相互作用,并将其在体外的阳性 cochaperone 活性转化为酵母生长促进作用,并帮助 Hsp70 折叠其客户 Ras 样蛋白。在特定 Hsp70/Bim 干扰物的帮助下,我们说明了 Hsp70/Bim 二聚体可将酵母从热休克中拯救出来。在缺乏凋亡 Bcl-2 因子的生物体中,哺乳动物细胞中的促凋亡 Bim 表现出促生存功能。
更新日期:2021-06-28
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