Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase

Sandra van Wilpe, Michael T. Ryan, Kerstin Hill, Ammy C. Maarse, Chris Meisinger, Jan Brix, Peter J. T. Dekker, Martin Moczko, Richard Wagner, Michiel Meijer, Bernard Guiard, Angelika Hönlinger and Nikolaus Pfanner ()
Additional contact information
Sandra van Wilpe: Institute for Molecular Cell Biology, BioCentrum Amsterdam
Michael T. Ryan: Institut für Biochemie und Molekularbiologie, Universität Freiburg
Kerstin Hill: Biophysik, Universität Osnabrück, FB Biologie/Chemie
Ammy C. Maarse: Institute for Molecular Cell Biology, BioCentrum Amsterdam
Chris Meisinger: Institut für Biochemie und Molekularbiologie, Universität Freiburg
Jan Brix: Institut für Biochemie und Molekularbiologie, Universität Freiburg
Peter J. T. Dekker: Institut für Biochemie und Molekularbiologie, Universität Freiburg
Martin Moczko: Institut für Biochemie und Molekularbiologie, Universität Freiburg
Richard Wagner: Biophysik, Universität Osnabrück, FB Biologie/Chemie
Michiel Meijer: Institute for Molecular Cell Biology, BioCentrum Amsterdam
Bernard Guiard: Centre de Génétique Moleculaire CNRS, Université Pierre et Marie Curie
Angelika Hönlinger: Institut für Biochemie und Molekularbiologie, Universität Freiburg
Nikolaus Pfanner: Institut für Biochemie und Molekularbiologie, Universität Freiburg

Nature, 1999, vol. 401, issue 6752, 485-489

Abstract: Abstract Mitochondrial preproteins are imported by a multisubunit translocase of the outer membrane (TOM), including receptor proteins and a general import pore1,2,3,4,5. The central receptor Tom22 binds preproteins through both its cytosolic domain and its intermembrane space domain6,7,8,9,10 and is stably associated with the channel protein Tom40 (refs 11,12,13). Here we report the unexpected observation that a yeast strain can survive without Tom22, although it is strongly reduced in growth and the import of mitochondrial proteins. Tom22 is a multifunctional protein that is required for the higher-level organization of the TOM machinery. In the absence of Tom22, the translocase dissociates into core complexes, representing the basic import units, but lacks a tight control of channel gating. The single membrane anchor of Tom22 is required for a stable interaction between the core complexes, whereas its cytosolic domain serves as docking point for the peripheral receptors Tom20 and Tom70. Thus a preprotein translocase can combine receptor functions with distinct organizing roles in a multidomain protein.

Date: 1999
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DOI: 10.1038/46802

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