An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae.
An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae.
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DOI：
10.1083/jcb.152.4.851
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发表时间：
2001-02-19
期刊：
影响因子：
--
通讯作者：
Craig EA
中科院分区：
文献类型：
--
作者：
Johnson JL;Craig EA
除了调节Hsp70的ATP酶循环，Hsp40的第二个关键作用已经基于体外研究提出：结合变性蛋白质底物，然后将其呈递给Hsp70进行折叠。然而，该模型的生物学重要性受到以下事实的挑战：只要保留Hsp70相互作用所需的区域，则酵母胞质溶胶的两个主要Hsp40中的任一个Ydj1和Sis1的底物结合结构域的缺失不会导致严重缺陷。作为该模型的体内测试，在具有两个Hsp40基因缺失的菌株中检查活力的要求。尽管序列相似性有限，但Sis1或Ydj1的底物结合结构域允许细胞生长，表明它们具有重叠的基本功能。此外，底物结合结构域必须与功能性Hsp70相互作用结构域顺式地起作用。我们的结论是，细胞溶质热休克蛋白40结合未折叠的蛋白质底物的能力是在体内的一个重要功能。
In addition to regulating the ATPase cycle of Hsp70, a second critical role of Hsp40s has been proposed based on in vitro studies: binding to denatured protein substrates, followed by their presentation to Hsp70 for folding. However, the biological importance of this model is challenged by the fact that deletion of the substrate-binding domain of either of the two major Hsp40s of the yeast cytosol, Ydj1 and Sis1, leads to no severe defects, as long as regions necessary for Hsp70 interaction are retained. As an in vivo test of this model, requirements for viability were examined in a strain having deletions of both Hsp40 genes. Despite limited sequence similarity, the substrate-binding domain of either Sis1 or Ydj1 allowed cell growth, indicating they share overlapping essential functions. Furthermore, the substrate-binding domain must function in cis with a functional Hsp70-interacting domain. We conclude that the ability of cytosolic Hsp40s to bind unfolded protein substrates is an essential function in vivo.
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影响因子：
64.5
作者：
GUARENTE, L;LALONDE, B;ALANI, E
通讯作者：
ALANI, E
DOI：
10.1083/jcb.114.4.623
发表时间：
1991-08
期刊：
The Journal of cell biology
影响因子：
--
作者：
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通讯作者：
Arndt KT
影响因子：
64.5
作者：
CAPLAN, AJ;CYR, DM;DOUGLAS, MG
通讯作者：
DOUGLAS, MG
影响因子：
64.5
作者：
ZHONG, T;ARNDT, KT
通讯作者：
ARNDT, KT
DOI：
10.1073/pnas.96.10.5452
发表时间：
1999-05-11
影响因子：
11.1
作者：
Laufen, T;Mayer, MP;Bukau, B
通讯作者：
Bukau, B