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© The Rockefeller University Press, 0021-9525/1999//973 $5.00
The Journal of Cell Biology, Volume 145, Number 5, , 1999 973-978

Direct Membrane Insertion of Voltage-dependent Anion-selective Channel Protein Catalyzed by Mitochondrial Tom20

Department of Biochemistry, McGill University, Montreal, Quebec, Canada H3G 1Y6

Insertion of newly synthesized proteins into or across the mitochondrial outer membrane is initiated by import receptors at the surface of the organelle. Typically, this interaction directs the precursor protein into a preprotein translocation pore, comprised of Tom40. Here, we show that a prominent β-barrel channel protein spanning the outer membrane, human voltage- dependent anion-selective channel (VDAC), bypasses the requirement for the Tom40 translocation pore during biogenesis. Insertion of VDAC into the outer membrane is unaffected by plugging the translocation pore with a partially translocated matrix preprotein, and mitochondria containing a temperature-sensitive mutant of Tom40 insert VDAC at the nonpermissive temperature. Synthetic liposomes harboring the cytosolic domain of the human import receptor Tom20 efficiently insert newly synthesized VDAC, resulting in transbilayer transport of ATP. Therefore, Tom20 transforms newly synthesized cytosolic VDAC into a transmembrane channel that is fully integrated into the lipid bilayer.

Key Words: voltage-dependent anion-selective channel • porin • Tom20 • import • mitochondria

Abbreviations used in this paper: DHFR, dihydrofolate reductase; GST, glutathione S-transferase; hTom20, human Tom20; LUVs, large unilamellar liposomes; MTX, methotrexate; pCOX Va, precytochrome oxidase subunit Va; PE, phosphatidylethanolamine; PE-pmbs, β-maleimidopropionic acid N-hydroxysuccinimide ester of PE; pOCT, preornithine carbamyl transferase; VDAC, voltage-dependent anion-selective channel.

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