Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria.

Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria.
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TOM40,是线粒体外膜中蛋白质传统的TOM通道的孔形成部分。

DOI:
10.1083/jcb.153.6.1151
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发表时间:
2001-06-11
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Nussberger S
Nussberger S
中科院分区:
其他
文献类型:
--
作者:
Ahting U;Thieffry M;Engelhardt H;Hegerl R;Neupert W;Nussberger S

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Tom 40是线粒体外膜前蛋白转位酶(TOM复合物)的主要成分。我们通过从纯化的TOM核心复合物中去除受体Tom 22和小的Tom组分Tom 6和Tom 7来分离粗糙脉孢菌的Tom 40。Tom 40是一个高分子量的复合物,分子量约为350 kD。它形成一个高电导通道。线粒体前序列肽与重构成平面脂质膜的Tom 40特异性相互作用,并以电压依赖性方式减少通过孔的离子流。通过圆二色性测量和傅里叶变换红外光谱测定,Tom 40的二级结构包括约31%的β-折叠、22%的α-螺旋和47%的剩余结构。纯化的Tom 40的电子显微镜检查显示主要具有一个染色累积中心的颗粒。它们可能代表一个直径约为2.5 nm的开孔,类似于TOM复合物中发现的孔。因此,Tom 40是TOM移位酶的核心元件;它在寡聚体组装中形成蛋白质传导通道。
Tom40 is the main component of the preprotein translocase of the outer membrane of mitochondria (TOM complex). We have isolated Tom40 of Neurospora crassa by removing the receptor Tom22 and the small Tom components Tom6 and Tom7 from the purified TOM core complex. Tom40 is organized in a high molecular mass complex of ∼350 kD. It forms a high conductance channel. Mitochondrial presequence peptides interact specifically with Tom40 reconstituted into planar lipid membranes and decrease the ion flow through the pores in a voltage-dependent manner. The secondary structure of Tom40 comprises ∼31% β-sheet, 22% α-helix, and 47% remaining structure as determined by circular dichroism measurements and Fourier transform infrared spectroscopy. Electron microscopy of purified Tom40 revealed particles primarily with one center of stain accumulation. They presumably represent an open pore with a diameter of ∼2.5 nm, similar to the pores found in the TOM complex. Thus, Tom40 is the core element of the TOM translocase; it forms the protein-conducting channel in an oligomeric assembly.
DOI: 10.1073/pnas.91.25.11973
发表时间: 1994-12-06
影响因子: 11.1
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