Mitochondrial Heat Shock Protein (Hsp) 70 and Hsp10 Cooperate in the Formation of Hsp60 Complexes
Mitochondrial Heat Shock Protein (Hsp) 70 and Hsp10 Cooperate in the Formation of Hsp60 Complexes
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DOI：
10.1074/jbc.m115.642017
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发表时间：
2015-05-01
影响因子：
4.8
通讯作者：
Becker, Thomas
中科院分区：
文献类型：
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作者：
Boettinger, Lena;Oeljeklaus, Silke;Becker, Thomas
线粒体Hsp70 （mtHsp70）介导线粒体生物发生的基本功能，如蛋白质的输入和折叠。在这些过程中，伴侣与同伴、前序转位酶和其他伴侣系统合作。伴侣蛋白Hsp60与其辅因子Hsp10一起催化mtHsp70客户蛋白子集的折叠。Hsp60形成七聚体环结构，为蛋白质折叠提供一个空腔。人们对Hsp60环是如何组装的知之甚少。在一项全面的相互作用研究中，我们发现mtHsp70与Hsp60和Hsp10相关。令人惊讶的是，mtHsp70独立于Hsp60与Hsp10相互作用。mtHsp70-Hsp10复合物与未组装的Hsp60前体结合，促进其组装成成熟的Hsp60复合物。我们得出结论，与Hsp10偶联可招募mtHsp70介导七聚体Hsp60环的生物发生。
Mitochondrial Hsp70 (mtHsp70) mediates essential functions for mitochondrial biogenesis, like import and folding of proteins. In these processes, the chaperone cooperates with cochaperones, the presequence translocase, and other chaperone systems. The chaperonin Hsp60, together with its cofactor Hsp10, catalyzes folding of a subset of mtHsp70 client proteins. Hsp60 forms heptameric ring structures that provide a cavity for protein folding. How the Hsp60 rings are assembled is poorly understood. In a comprehensive interaction study, we found that mtHsp70 associates with Hsp60 and Hsp10. Surprisingly, mtHsp70 interacts with Hsp10 independently of Hsp60. The mtHsp70-Hsp10 complex binds to the unassembled Hsp60 precursor to promote its assembly into mature Hsp60 complexes. Weconclude that coupling to Hsp10 recruits mtHsp70 to mediate the biogenesis of the heptameric Hsp60 rings.