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蛋白质导入酵母线粒体基质。线粒体内外膜之间一种新的易位中间体。

Protein import into the yeast mitochondrial matrix. A new translocation intermediate between the two mitochondrial membranes.

作者信息

Hwang S T, Wachter C, Schatz G

机构信息

Biocenter, University of Basel, Switzerland.

出版信息

J Biol Chem. 1991 Nov 5;266(31):21083-9.

PMID:1657948
Abstract

Import of authentic or artificial precursor proteins into the matrix of isolated yeast mitochondria can proceed via a translocation intermediate that is lodged between the two mitochondrial membranes. The intermediate accumulates when import is arrested by depleting mitochondria of ATP. Generation of the intermediate requires a potential across the inner membrane. The intermediate is membrane-bound, partly or completely processed (depending on the precursor), and chased into the matrix by added ATP. This chase does not require a potential across the inner membrane. The properties of this intermediate support the proposal (Hwang, S., Jascur, J., Vestweber, D., Pon, L., and Schatz, G. (1989) J. Cell Biol. 109, 487-493) that import into the matrix involves two distinct translocation systems in the outer and the inner mitochondrial membrane that are not permanently coupled to each other. Only translocation across the inner membrane requires ATP in the matrix.

摘要

将真实的或人工合成的前体蛋白导入分离的酵母线粒体基质中可通过一种位于两个线粒体膜之间的易位中间体进行。当通过耗尽线粒体中的ATP来阻止导入时,该中间体会积累。中间体的产生需要内膜两侧的电位。该中间体与膜结合,部分或完全被加工(取决于前体),并通过添加ATP被追踪到基质中。这种追踪不需要内膜两侧的电位。该中间体的特性支持了以下提议(Hwang, S., Jascur, J., Vestweber, D., Pon, L., and Schatz, G. (1989) J. Cell Biol. 109, 487 - 493),即导入基质涉及线粒体外膜和内膜中两个不同的易位系统,它们并非永久相互偶联。只有跨内膜的易位需要基质中的ATP。

相似文献

1
Protein import into the yeast mitochondrial matrix. A new translocation intermediate between the two mitochondrial membranes.蛋白质导入酵母线粒体基质。线粒体内外膜之间一种新的易位中间体。
J Biol Chem. 1991 Nov 5;266(31):21083-9.
2
Sequential translocation of an artificial precursor protein across the two mitochondrial membranes.人工前体蛋白依次穿过线粒体的两层膜。
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The requirement of matrix ATP for the import of precursor proteins into the mitochondrial matrix and intermembrane space.基质ATP对于前体蛋白导入线粒体基质和膜间隙的需求。
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Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane.介导前体蛋白穿过线粒体内膜转运的各组分间的多重相互作用。
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Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22.由Tim22介导的载体蛋白导入线粒体内膜。
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Precursor proteins in transit through mitochondrial contact sites interact with hsp70 in the matrix.通过线粒体接触位点转运的前体蛋白与基质中的热休克蛋白70相互作用。
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引用本文的文献

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Life (Basel). 2021 May 11;11(5):432. doi: 10.3390/life11050432.
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Adaptation of a Genetic Screen Reveals an Inhibitor for Mitochondrial Protein Import Component Tim44.一项遗传筛选的适应性研究揭示了一种线粒体蛋白输入组件Tim44的抑制剂。
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Models of post-translational protein translocation.
蛋白质翻译后转运模型。
Biophys J. 2000 Nov;79(5):2235-51. doi: 10.1016/S0006-3495(00)76471-X.
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The dimensions of the protein import channels in the outer and inner mitochondrial membranes.线粒体外膜和内膜中蛋白质输入通道的尺寸。
Proc Natl Acad Sci U S A. 1999 Nov 9;96(23):13086-90. doi: 10.1073/pnas.96.23.13086.
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Separation of structural and dynamic functions of the mitochondrial translocase: Tim44 is crucial for the inner membrane import sites in translocation of tightly folded domains, but not of loosely folded preproteins.线粒体转位酶结构与动态功能的分离:Tim44对于紧密折叠结构域转位时内膜导入位点至关重要,但对松散折叠前体蛋白的转位并非如此。
EMBO J. 1998 Aug 3;17(15):4226-37. doi: 10.1093/emboj/17.15.4226.
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Strong precursor-pore interactions constrain models for mitochondrial protein import.强大的前体-孔相互作用限制了线粒体蛋白质导入模型。
Biophys J. 1998 Apr;74(4):1732-43. doi: 10.1016/S0006-3495(98)77884-1.
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EMBO J. 1997 Nov 17;16(22):6727-36. doi: 10.1093/emboj/16.22.6727.
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In vivo zippering of inner and outer mitochondrial membranes by a stable translocation intermediate.通过稳定的易位中间体实现线粒体内外膜的体内拉链式连接。
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Analysis of the sorting signals directing NADH-cytochrome b5 reductase to two locations within yeast mitochondria.指导NADH-细胞色素b5还原酶定位于酵母线粒体内两个位置的分选信号分析。
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Role of the intermembrane-space domain of the preprotein receptor Tom22 in protein import into mitochondria.前体蛋白受体Tom22的膜间隙结构域在蛋白质导入线粒体中的作用。
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