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  The preprotein translocation channel of the outer membrane of mitochondria

Kunkele, K. P., Heins, S., Dembowski, M., Nargang, F. E., Benz, R., Thieffry, M., et al. (1998). The preprotein translocation channel of the outer membrane of mitochondria. Cell, 93(6), 1009-1019.

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Kunkele, K. P., Author
Heins, S., Author
Dembowski, M., Author
Nargang, F. E., Author
Benz, R., Author
Thieffry, M., Author
Walz, J.1, Author              
Lill, R., Author
Nussberger, S., Author
Neupert, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Endoplasmic-reticulum membrane; Protein import receptor; General insertion pore; Precursor proteins; Escherichia-coli; Neurospora-crassa; Secretory proteins; Cationic channel; Cell viability; Complex.; Cell & developmental biology.
 Abstract: The preprotein translocase of the outer membrane of mitochondria (TOM complex) facilitates the recognition, insertion, and translocation of nuclear-encoded mitochondrial preproteins. We have purified the TOM complex from Neurospora crassa and analyzed its composition and functional properties. The TOM complex contains a cation-selective high-conductance channel. Upon reconstitution into liposomes, it mediates integration of proteins into and translocation across the lipid bilayer. TOM complex particles have a diameter of about 138 Angstrom, as revealed by electron microscopy and image analysis; they contain two or three centers of stain-filled openings, which we interpret as pores with an apparent diameter of about 20 Angstrom. We conclude that the structure reported here represents the protein-conducting channel of the mitochondrial outer membrane. [References: 75]

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 Dates: 1998-06-12
 Publication Status: Published in print
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 Identifiers: eDoc: 318677
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Title: Cell
Source Genre: Journal
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Pages: - Volume / Issue: 93 (6) Sequence Number: - Start / End Page: 1009 - 1019 Identifier: -