Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase

Article Abstract:

It has been possible to identify a new principle of organization of a multi-subunit preprotein translocase. It was found that the multidomain protein Tom22, required for the higher-level organization of the translocase of the outer membrane machinery, acts not only acts as a receptor and trans binding site for preproteins, but also organizes the interaction between the channel and receptor subcomplexes at two levels. It was also established that Tom22 is needed to negatively regulate the open probability of the Tom40 channel.

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Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins

Article Abstract:

The mitochondrial outer membrane controls the import of preproteins encoded by nuclear genes. Eight different translocase of outer membrane (Tom) proteins that function as receptors have been identified. The expression and functional reconstitution of Tom40 which is an integral membrane protein, is reported. It forms a cation-selective high conductance channel, binding specifically to and transporting mitochondrial-targeting sequences.

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Machinery for protein sorting and assembly in the mitochondrial outer membrane

Article Abstract:

The authors have investigated mitochondrial outer membrane. They report that this membrane contains an assembly and sorting machinery operating after outer membrane translocase.

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