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Mitochondrial inner membrane protease promotes assembly of presequence translocase by removing a carboxy-terminal targeting sequence

Author

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  • Raffaele Ieva

    (Institut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg)

  • Anna K. Heißwolf

    (Institut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg
    Present address: Roche Diagnostics, Pharma Research and Early Development, 82377 Penzberg, Germany)

  • Michael Gebert

    (Institut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg
    Faculty of Biology, Universität Freiburg
    Present address: Harvard Medical School, Department of Neurobiology, Boston, Massachusetts 02115, USA)

  • F.-Nora Vögtle

    (Institut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg)

  • Florian Wollweber

    (Institut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg)

  • Carola S. Mehnert

    (Institut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg
    Faculty of Biology, Universität Freiburg)

  • Silke Oeljeklaus

    (BIOSS Centre for Biological Signalling Studies, Universität Freiburg
    Institut für Biologie II, Fakultät für Biologie, Funktionelle Proteomik, Universität Freiburg)

  • Bettina Warscheid

    (BIOSS Centre for Biological Signalling Studies, Universität Freiburg
    Institut für Biologie II, Fakultät für Biologie, Funktionelle Proteomik, Universität Freiburg)

  • Chris Meisinger

    (Institut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg
    BIOSS Centre for Biological Signalling Studies, Universität Freiburg)

  • Martin van der Laan

    (Institut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg
    Collaborative Research Centre for Functional Specificity, Universität Freiburg)

  • Nikolaus Pfanner

    (Institut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg
    BIOSS Centre for Biological Signalling Studies, Universität Freiburg)

Abstract

The presequence translocase of the inner mitochondrial membrane (TIM23 complex) is essential for importing cleavable preproteins into mitochondria. The preproteins contain amino-terminal targeting sequences that are removed by the mitochondrial processing peptidase (MPP). Some preproteins carry bipartite presequences that are cleaved twice, by MPP and the inner membrane protease (IMP). Here, we report that the TIM23 complex is altered in mitochondria lacking the IMP subunit Imp1 although none of the TIM23 components contains a bipartite presequence. We show that the TIM23 subunit Mgr2 is processed by IMP, but not by MPP. The cytosolic precursor of Mgr2 contains a carboxy-terminal sequence that promotes targeting to mitochondria, but impairs stable assembly and function of the mature TIM23 complex. IMP removes the carboxy-terminal targeting sequence and thus promotes proper assembly of the TIM23 complex. Our results reveal carboxy-terminal processing as a new mechanism in the biogenesis of the mitochondrial inner membrane.

Suggested Citation

  • Raffaele Ieva & Anna K. Heißwolf & Michael Gebert & F.-Nora Vögtle & Florian Wollweber & Carola S. Mehnert & Silke Oeljeklaus & Bettina Warscheid & Chris Meisinger & Martin van der Laan & Nikolaus Pfa, 2013. "Mitochondrial inner membrane protease promotes assembly of presequence translocase by removing a carboxy-terminal targeting sequence," Nature Communications, Nature, vol. 4(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3853
    DOI: 10.1038/ncomms3853
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