Interaction of client-the scaffold on which FeS clusters are build-with J-domain protein Hsc20 and its evolving Hsp70 partners.
Interaction of client-the scaffold on which FeS clusters are build-with J-domain protein Hsc20 and its evolving Hsp70 partners.
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DOI：
10.3389/fmolb.2022.1034453
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发表时间：
2022
影响因子：
5
通讯作者：
中科院分区：
文献类型：
--
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在细胞中，由Hsp70及其必需的J结构域蛋白(JDP)组成的分子伴侣系统与大量客户蛋白瞬时相互作用-JDP通常招募他们的伴侣Hsp70与特定客户相互作用。JDP/Hsp70系统与客户之间这种周期性互动的基本原理已经确立。人们对JDP/Hsp70系统功能的其他方面知之甚少，包括这种系统如何随着时间的推移而演变。在这里，我们讨论了JDP/Hsp70系统在铁-硫团簇(FeS)生物发生中的作用。客户蛋白是构建集群的支架，它与其专门的JDP Hsc20之间的相互作用保持不变。然而，该系统的Hsp70至少更换了两次。在一些物种中，Hsc20的S Hsp70伴侣只与支架相互作用，而在另一些物种中，除Hsc20外，它还有许多JDP伴侣，并与许多客户蛋白相互作用。对HSP70合作伙伴的这种切换的分析已经洞察到当一个蜂窝隔间中存在多个HSP70时，JDP/HSP70系统之间可能发生的相互隔离，以及当一个HSP70合作伙伴在多个DDP之间共享时，如何平衡JDP/HSP70系统之间的竞争。具有特别广泛的相关性，尽管支架与Hsc20和Hsp70的相互作用在功能上对含有FeS簇的蛋白质的生物发生至关重要，但正是Hsc20-Hsp70相互作用本身的调节使Hsc20能够与如此不同的Hsp70伙伴一起发挥作用。
In cells molecular chaperone systems consisting of Hsp70 and its obligatory J-domain protein (JDP) co-chaperones transiently interact with a myriad of client proteins—with JDPs typically recruiting their partner Hsp70 to interact with particular clients. The fundamentals of this cyclical interactions between JDP/Hsp70 systems and clients are well established. Much less is known about other aspects of JDP/Hsp70 system function, including how such systems evolved over time. Here we discuss the JDP/Hsp70 system involved in the biogenesis of iron-sulfur (FeS) clusters. Interaction between the client protein, the scaffold on which clusters are built, and its specialized JDP Hsc20 has stayed constant. However, the system’s Hsp70 has changed at least twice. In some species Hsc20’s Hsp70 partner interacts only with the scaffold, in others it has many JDP partners in addition to Hsc20 and interacts with many client proteins. Analysis of this switching of Hsp70 partners has provided insight into the insulation of JDP/Hsp70 systems from one another that can occur when more than one Hsp70 is present in a cellular compartment, as well as how competition among JDPs is balanced when an Hsp70 partner is shared amongst a number of JDPs. Of particularly broad relevance, even though the scaffold’s interactions with Hsc20 and Hsp70 are functionally critical for the biogenesis of FeS cluster-containing proteins, it is the modulation of the Hsc20-Hsp70 interaction per se that allows Hsc20 to function with such different Hsp70 partners.
DOI：
10.1083/jcb.134.3.603
发表时间：
1996-08
期刊：
The Journal of cell biology
影响因子：
--
作者：
Schilke B;Forster J;Davis J;James P;Walter W;Laloraya S;Johnson J;Miao B;Craig E
通讯作者：
Craig E