Dynamics of the preprotein translocation channel of the outer membrane of mitochondria.

ABSTRACT: The protein translocase of the outer mitochondrial membrane (TOM) serves as the main entry site for virtually all mitochondrial proteins. Like many other protein translocases it also has an ion channel activity that can be used to study the dynamical properties of this supramolecular complex. We have purified TOM core complex and Tom40, the main pore forming subunit, from mitochondria of the filamentous fungus Neurospora crassa and incorporated them into planar lipid bilayers. We then examined their single channel properties to provide a detailed description of the conformational dynamics of this channel in the absence of its protein substrate. For isolated TOM core complex we have found at least six conductance states. Transitions between these states were voltage-dependent with a bell-sh

SUBMITTER: Poynor M 

PROVIDER: S-EPMC2479589 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature