Evolutionary conservation of biogenesis of β-barrel membrane proteins

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Abstract
The outer membranes of mitochondria and chloroplasts are distinguished by the presence of β-barrel membrane proteins1,2. The outer membrane of Gram-negative bacteria also harbours β-barrel proteins3. In mitochondria these proteins fulfil a variety of functions such as transport of small molecules (porin/VDAC), translocation of proteins (Tom40) and regulation of mitochondrial morphology (Mdm10)4,5,6,7. These proteins are encoded by the nucleus, synthesized in the cytosol, targeted to mitochondria as chaperone-bound species, recognized by the translocase of the outer membrane, and then inserted into the outer membrane where they assemble into functional oligomers8,9,10,11. Whereas some knowledge has been accumulated on the pathways of insertion of proteins that span cellular membranes with α-helical segments, very little is known about how β-barrel proteins are integrated into lipid bilayers and assembled into oligomeric structures12. Here we describe a protein complex that is essential for the topogenesis of mitochondrial outer membrane β-barrel proteins (TOB). We present evidence that important elements of the topogenesis of β-barrel membrane proteins have been conserved during the evolution of mitochondria from endosymbiotic bacterial ancestors13.