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:
影响因子:
--
通讯作者:
Nussberger S
中科院分区:
文献类型:
--
作者:
Ahting U;Thieffry M;Engelhardt H;Hegerl R;Neupert W;Nussberger S
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.
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DOI:
10.1073/pnas.91.25.11973
发表时间:
1994-12-06
影响因子:
11.1
作者:
LITHGOW, T;JUNNE, T;SCHATZ, G
通讯作者:
SCHATZ, G
影响因子:
11.4
作者:
HINES, V;BRANDT, A;SCHATZ, G
通讯作者:
SCHATZ, G
影响因子:
7.8
作者:
Ahting, U;Thun, C;Hegerl, R;Typke, D;Nargang, F E;Neupert, W;Nussberger, S
通讯作者:
Nussberger, S
影响因子:
64.8
作者:
Dietmeier, K;Honlinger, A;Pfanner, N
通讯作者:
Pfanner, N
影响因子:
5.3
作者:
Dekker, PJT;Ryan, MT;Pfanner, N
通讯作者:
Pfanner, N