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Science 9 June 2006:
Vol. 312. no. 5779, pp. 1523 - 1526
DOI: 10.1126/science.1127628
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Reports
Tim50 Maintains the Permeability Barrier of the Mitochondrial Inner Membrane
Michael Meinecke,1
Richard Wagner,1*
Peter Kovermann,1
Bernard Guiard,2
David U. Mick,3
Dana P. Hutu,3,4
Wolfgang Voos,3
Kaye N. Truscott,3,5
Agnieszka Chacinska,3
Nikolaus Pfanner,3*
Peter Rehling3
Transport of metabolites across the mitochondrial inner membrane is highly selective, thereby maintaining the electrochemical proton gradient that functions as the main driving force for cellular adenosine triphosphate synthesis. Mitochondria import many preproteins via the presequence translocase of the inner membrane. However, the reconstituted Tim23 protein constitutes a pore remaining mainly in its open form, a state that would be deleterious in organello. We found that the intermembrane space domain of Tim50 induced the Tim23 channel to close. Presequences overcame this effect and activated the channel for translocation. Thus, the hydrophilic cis domain of Tim50 maintains the permeability barrier of mitochondria by closing the translocation pore in a presequence-regulated manner.
1 Biophysik, Universität Osnabrück, FB Biologie/Chemie, D-49034 Osnabrück, Germany.
2 Centre de Génétique Moléculaire, Laboratoire propre du CNRS, F-91190 Gif-sur-Yvette, France.
3 Institut für Biochemie und Molekularbiologie, Universität Freiburg, Hermann-Herder-Straße 7, D-79104 Freiburg, Germany.
4 Fakultät für Biologie, Universität Freiburg, Schänzlestraße 1, D-79104 Freiburg, Germany.
5 Department of Biochemistry, La Trobe University, Melbourne 3086, Australia.
 Present address: Institute for Plant Biology, Molecular Physiology, University of Zürich, 8008 Zürich, Switzerland.
* To whom correspondence should be addressed. E-mail: wagner{at}biologie.uni-osnabrueck.de (R.W.); nikolaus.pfanner{at}biochemie.uni-freiburg.de (N.P.)
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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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- D. P. Hutu, B. Guiard, A. Chacinska, D. Becker, N. Pfanner, P. Rehling, and M. van der Laan (2008)
Mol. Biol. Cell
19, 2642-2649
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- Quaternary Structure of the Mitochondrial TIM23 Complex Reveals Dynamic Association between Tim23p and Other Subunits.
- N. N. Alder, J. Sutherland, A. I. Buhring, R. E. Jensen, and A. E. Johnson (2008)
Mol. Biol. Cell
19, 159-170
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- Sorting switch of mitochondrial presequence translocase involves coupling of motor module to respiratory chain.
- N. Wiedemann, M. van der Laan, D. P. Hutu, P. Rehling, and N. Pfanner (2007)
J. Cell Biol.
179, 1115-1122
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- The Interplay between Components of the Mitochondrial Protein Translocation Motor Studied Using Purified Components.
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282, 33935-33942
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- S. Kutik, B. Guiard, H. E. Meyer, N. Wiedemann, and N. Pfanner (2007)
J. Cell Biol.
179, 585-591
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- Awaking TIM22, a Dynamic Ligand-gated Channel for Protein Insertion in the Mitochondrial Inner Membrane.
- P. M. V. Peixoto, F. Grana, T. J. Roy, C. D. Dunn, M. Flores, R. E. Jensen, and M. L. Campo (2007)
J. Biol. Chem.
282, 18694-18701
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- Involvement of the Mitochondrial Protein Translocator Component Tim50 in Growth, Cell Proliferation and the Modulation of Respiration in Drosophila.
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176, 927-936
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- A conserved phosphatase cascade that regulates nuclear membrane biogenesis.
- Y. Kim, M. S. Gentry, T. E. Harris, S. E. Wiley, J. C. Lawrence Jr, and J. E. Dixon (2007)
PNAS
104, 6596-6601
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- Tim17p Regulates the Twin Pore Structure and Voltage Gating of the Mitochondrial Protein Import Complex TIM23.
- S. Martinez-Caballero, S. M. Grigoriev, J. M. Herrmann, M. L. Campo, and K. W. Kinnally (2007)
J. Biol. Chem.
282, 3584-3593
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- The Pam18/Tim14-Pam16/Tim16 complex of the mitochondrial translocation motor: The formation of a stable complex from marginally stable proteins.
- O. Iosefson, R. Levy, M. Marom, O. Slutsky-Leiderman, and A. Azem (2007)
Protein Sci.
16, 316-322
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- Evolution of the molecular machines for protein import into mitochondria..
- P. Dolezal, V. Likic, J. Tachezy, and T. Lithgow (2006)
Science
313, 314-318
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