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

Ahting, U., Thieffry, M., Engelhardt, H., Hegerl, R., Neupert, W., & Nussberger, S. (2001). Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria. Journal of Cell Biology, 153(6), 1151-1160.

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Genre: Journal Article
Alternative Title : J. Cell Biol

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Ahting, U., Author
Thieffry, M., Author
Engelhardt, H.1, Author              
Hegerl, R.1, Author              
Neupert, W.1, Author              
Nussberger, S., Author
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1External Organizations, ou_persistent22              

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Free keywords: Tom complex; Tom40; Mitochondria; Protein translocation channel; Protein targeting.; General insertion pore; Receptor complex; Import pore; Preprotein translocase; Secondary structure; Precursor proteins; Circular-dichroism; Neurospora-crassa; Yeast; Mom22.; Cell & Developmental Biology in Current Contents(R)/Life Sciences.
 Abstract: 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 similar to 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 similar to 31% beta -sheet, 22% alpha -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 similar to2.5 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. [References: 49]

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 Dates: 2001
 Publication Status: Published in print
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 Identifiers: eDoc: 318506
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Title: Journal of Cell Biology
  Alternative Title : J. Cell Biol
Source Genre: Journal
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Pages: - Volume / Issue: 153 (6) Sequence Number: - Start / End Page: 1151 - 1160 Identifier: -