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

Kerstin Hill, Kirstin Model, Michael T. Ryan, Klaus Dietmeier, Falk Martin, Richard Wagner and Nikolaus Pfanner ()
Additional contact information
Kerstin Hill: Biophysik, Universität Osnabrück, FB Biologie/Chemie
Kirstin Model: Institut für Biochemie und Molekularbiologie, Universität Freiburg
Michael T. Ryan: Institut für Biochemie und Molekularbiologie, Universität Freiburg
Klaus Dietmeier: Institut für Biochemie und Molekularbiologie, Universität Freiburg
Falk Martin: Institut für Biochemie und Molekularbiologie, Universität Freiburg
Richard Wagner: Biophysik, Universität Osnabrück, FB Biologie/Chemie
Nikolaus Pfanner: Institut für Biochemie und Molekularbiologie, Universität Freiburg

Nature, 1998, vol. 395, issue 6701, 516-521

Abstract: Abstract The mitochondrial outer membrane contains machinery for the import of preproteins encoded by nuclear genes1,2,3. Eight different Tom (translocase of outer membrane) proteins have been identified that function as receptors and/or are related to a hypothetical general import pore. Many mitochondrial membrane channel activities have been described4,5,6,7, including one related to Tim23 of the inner-membrane protein-import system5; however, the pore-forming subunit(s) of the Tom machinery have not been identified until now. Here we describe the expression and functional reconstitution of Tom40, an integral membrane protein with mainly β-sheet structure. Tom40 forms a cation-selective high-conductance channel that specifically binds to and transports mitochondrial-targeting sequences added to the cis side of the membrane. We conclude that Tom40 is the pore-forming subunit of the mitochondrial general import pore and that it constitutes a hydrophilic, ∼22 Å wide channel for the import of preproteins.

Date: 1998
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DOI: 10.1038/26780

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