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The preprotein translocation channel of the outer membrane of mitochondria.

Authors
  • Künkele, K P1
  • Heins, S
  • Dembowski, M
  • Nargang, F E
  • Benz, R
  • Thieffry, M
  • Walz, J
  • Lill, R
  • Nussberger, S
  • Neupert, W
  • 1 Institut für Physiologische Chemie, Physikalische Biochemie, und Zellbiologie der Universität München, Germany.
Type
Published Article
Journal
Cell
Publisher
Elsevier
Publication Date
Jun 12, 1998
Volume
93
Issue
6
Pages
1009–1019
Identifiers
PMID: 9635430
Source
Medline
License
Unknown

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 A, 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 A. We conclude that the structure reported here represents the protein-conducting channel of the mitochondrial outer membrane.

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