Mitochondrial protein import in trypanosomatids: Variations on a theme or fundamentally different?
Fig 2
Comparison between the MIM complex of S. cerevisiae and pATOM36 of T. brucei.
The two complexes that are required for the biogenesis of a subset of OM proteins including subunits of the TOM and ATOM complexes, respectively. The MIM complex consists of Mim1 and Mim2, neither of which shows sequence similarity with pATOM36. Although pATOM36 is an integral membrane protein, its two predicted transmembrane domains have not yet been confirmed experimentally. pATOM36 is dually localized all over the OM and in the TAC (box with dashed lines) that links the mitochondrial DNA with the basal body of the flagellum. Therefore, pATOM36 has an essential function in OM protein biogenesis and as an essential component of the TAC in the segregation of the replicated single unit kDNA of T. brucei. kDNA, kinetoplast DNA; MIM, mitochondrial import machinery; OM, outer membrane; pATOM36, peripheral ATOM of 36 kDa; TAC, tripartite attachment complex.