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Characterization of the targeting signal in mitochondrial β-barrel proteins

Tobias Jores, Anna Klinger, Lucia E. Groß, Shin Kawano, Nadine Flinner, Elke Duchardt-Ferner, Jens Wöhnert, Hubert Kalbacher, Toshiya Endo, Enrico Schleiff () and Doron Rapaport ()
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Tobias Jores: Interfaculty Institute of Biochemistry, University of Tuebingen
Anna Klinger: Molecular Cell Biology of Plants, Goethe University
Lucia E. Groß: Molecular Cell Biology of Plants, Goethe University
Shin Kawano: Faculty of Life Sciences, Kyoto Sangyo University
Nadine Flinner: Molecular Cell Biology of Plants, Goethe University
Elke Duchardt-Ferner: Institute for Molecular Biosciences, Center for Biomolecular Magnetic Resonance, Goethe University
Jens Wöhnert: Institute for Molecular Biosciences, Center for Biomolecular Magnetic Resonance, Goethe University
Hubert Kalbacher: Interfaculty Institute of Biochemistry, University of Tuebingen
Toshiya Endo: Faculty of Life Sciences, Kyoto Sangyo University
Enrico Schleiff: Molecular Cell Biology of Plants, Goethe University
Doron Rapaport: Interfaculty Institute of Biochemistry, University of Tuebingen

Nature Communications, 2016, vol. 7, issue 1, 1-16

Abstract: Abstract Mitochondrial β-barrel proteins are synthesized on cytosolic ribosomes and must be specifically targeted to the organelle before their integration into the mitochondrial outer membrane. The signal that assures such precise targeting and its recognition by the organelle remained obscure. In the present study we show that a specialized β-hairpin motif is this long searched for signal. We demonstrate that a synthetic β-hairpin peptide competes with the import of mitochondrial β-barrel proteins and that proteins harbouring a β-hairpin peptide fused to passenger domains are targeted to mitochondria. Furthermore, a β-hairpin motif from mitochondrial proteins targets chloroplast β-barrel proteins to mitochondria. The mitochondrial targeting depends on the hydrophobicity of the β-hairpin motif. Finally, this motif interacts with the mitochondrial import receptor Tom20. Collectively, we reveal that β-barrel proteins are targeted to mitochondria by a dedicated β-hairpin element, and this motif is recognized at the organelle surface by the outer membrane translocase.

Date: 2016
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12036

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DOI: 10.1038/ncomms12036

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