| Literature DB >> 9635430 |
K P Künkele1, S Heins, M Dembowski, F E Nargang, R Benz, M Thieffry, J Walz, R Lill, S Nussberger, W Neupert.
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.Entities:
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Year: 1998 PMID: 9635430 DOI: 10.1016/s0092-8674(00)81206-4
Source DB: PubMed Journal: Cell ISSN: 0092-8674 Impact factor: 41.582