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Mitochondrial Import Driving Forces: Enhanced Trapping by Matrix Hsp70 Stimulates Translocation and Reduces the Membrane Potential Dependence of Loosely Folded Preproteins

机译：线粒体导入驱动力：基质Hsp70增强的诱捕刺激易位并减少了折叠前蛋白的膜电位依赖性。

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The mitochondrial heat shock protein Hsp70 (mtHsp70) is essential for driving translocation of preproteins into the matrix. Two models, trapping and pulling by mtHsp70, are discussed, but positive evidence for either model has not been found so far. We have analyzed a mutant mtHsp70, Ssc1-2, that shows a reduced interaction with the membrane anchor Tim44, but an enhanced trapping of preproteins. Unexpectedly, at a low inner membrane potential, ssc1-2 mitochondria imported loosely folded preproteins more efficiently than wild-type mitochondria. The import of a tightly folded preprotein, however, was not increased in ssc1-2 mitochondria. Thus, enhanced trapping by mtHsp70 stimulates the import of loosely folded preproteins and reduces the dependence on the import-driving activity of the membrane potential, directly demonstrating that trapping is one of the molecular mechanisms of mtHsp70 action.

机译：线粒体热休克蛋白Hsp70（mtHsp70）对于驱动前蛋白向基质的转运至关重要。讨论了两种模型，分别是mtHsp70的诱捕和拉动，但是到目前为止，尚未找到任何一种模型的积极证据。我们已经分析了一个突变型mtHsp70 Ssc1-2，该突变型与膜锚Tim44的相互作用降低，但对前蛋白的捕获增强。出乎意料的是，在低内膜电位下，ssc1-2线粒体比野生型线粒体更有效地导入松散折叠的前蛋白。但是，在ssc1-2线粒体中，紧密折叠的前蛋白的进口没有增加。因此，由mtHsp70增强的捕获刺激了松散折叠的前蛋白的导入，并减少了对膜电位的导入驱动活性的依赖性，直接证明了捕获是mtHsp70作用的分子机制之一。

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期刊名称 Molecular and Cellular Biology
作者
Andreas Geissler; Joachim Rassow; Nikolaus Pfanner; Wolfgang Voos;
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作者单位

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年(卷),期 2001(21),20
年度 2001
页码 7097–7104
总页数 8
原文格式 PDF
正文语种
中图分类分子生物学;细胞生物学;
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1. Mitochondrial Import Driving Forces: Enhanced Trapping by Matrix Hsp70 Stimulates Translocation and Reduces the Membrane Potential Dependence of Loosely Folded Preproteins [J] . Andreas Geissler, Joachim Rassow, Nikolaus Pfanner, Molecular and Cellular Biology . 2001,第20期

机译：线粒体导入驱动力：基质Hsp70增强的诱捕刺激易位，并降低了折叠前蛋白的膜电位依赖性。
2. Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins. [J] . S Laloraya, P J Dekker, W Voos, Molecular and Cellular Biology . 1995,第12期

机译：线粒体GrpE调节基质Hsp70在前蛋白易位和成熟中的功能。
3. A Cooperative Action of the ATP-Dependent Import Motor Complex and the Inner Membrane Potential Drives Mitochondrial Preprotein Import [J] . Martin Krayl, Joo Hyun Lim, Falk Martin, Molecular and Cellular Biology . 2007,第2期

机译：ATP依赖进口运动复合体和内膜电位的协同作用驱动线粒体前蛋白的进口。
4. 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. [O] . U Bömer, A C Maarse, F Martin, 1998

机译：线粒体转座酶的结构和动态功能的分离：Tim44对于内膜导入位点在紧折叠结构域而不是松散折叠前蛋白易位中至关重要。
5. Mitochondrial Import Driving Forces: Enhanced Trapping by Matrix Hsp70 Stimulates Translocation and Reduces the Membrane Potential Dependence of Loosely Folded Preproteins [O] . Geissler, Andreas, Rassow, Joachim, Pfanner, Nikolaus, 2001

机译：线粒体导入驱动力：基质Hsp70增强的诱捕刺激易位，并减少了折叠前蛋白的膜电位依赖性。
6. The Force Exerted by the Membrane Potential During Protein Import into the Mitochondrial Matrix [R] . Shariff, Karim, Ghosal, Sandip, Matouschek, Andreas 2002

机译：蛋白质导入线粒体基质过程中膜电位的作用力

Mitochondrial Import Driving Forces: Enhanced Trapping by Matrix Hsp70 Stimulates Translocation and Reduces the Membrane Potential Dependence of Loosely Folded Preproteins

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