The preprotein translocation channel of the outer membrane of mitochondria

Kunkele, K. P.; Heins, S.; Dembowski, M.; Nargang, F. E.; Benz, R.; Thieffry, M.; Walz, J.; Lill, R.; Nussberger, S.; Neupert, W.

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

The preprotein translocation channel of the outer membrane of mitochondria

MPS-Authors

There are no MPG-Authors in the publication available

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

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.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-7209-A

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]