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A preprotein is stably arrested and accumulated in the GIP complex by Tom40 and Tom22.4 Such a 100 kDa core complex probably contains a single channel that retains the basic channel properties but is already open in the absence of preproteins. In contrast, in the presence of Tom22, the wild-type GIP complex contains tightly regulated channels (probably three channels). Tom22 apparently represents a component of the machinery that controls the gate. The cytosolic domains of Tom22 and Tom20 are believed to form the major part of a cis site, which mediates the import of all preproteins known to use the general import machinery of mitochondria. The preprotein is then routed through the Tom complex translocation channel and transferred to a trans site on the intermembrane space (IMS) side of the outer membrane. The inter-membrane space exposed segment of Tom40 and the C-terminal tail of Tom22 may contribute to the trans-site. Matrix-targeted proteins are further transferred to the matrix through Product Information import machinery in the inner membrane.

The TOM complex of mammalian mitochondria resembles the fungal Tom complex, but is distinct from the plant TOM system. Thus, while unique components of the mammalian mitochondrial import system have been identified (e.g. TOM34 and metaxin), Tom22, and Tom37 have not been identified in plant mitochondria.






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