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Tom5 functionally links mitochondrial preprotein receptors to the general import pore

Author

Listed:
  • Klaus Dietmeier
  • Angelika Hönlinger
  • Ulf Bömer

    (Institut für Biochemie und Molekularbiologie, Universität Freiburg)

  • Peter J. T. Dekker

    (Institut für Biochemie und Molekularbiologie, Universität Freiburg)

  • Christoph Eckerskorn

    (†Max-Planck-Institut für Biochemie)

  • Fritz Lottspeich

    (†Max-Planck-Institut für Biochemie)

  • Michael Kübrich

    (Institut für Biochemie und Molekularbiologie, Universität Freiburg)

  • Nikolaus Pfanner

    (Institut für Biochemie und Molekularbiologie, Universität Freiburg)

Abstract

Most mitochondrial proteins are synthesized as preproteins on cytosolic polysomes and are subsequently imported into the organelle1,2,3. The mitochondrial outer membrane contains a multisubunit preprotein translocase (Tom) which has receptors on the cytosolic side and a general import pore (GIP) in the membrane. Tom20–Tom22 and Tom70–Tom37 function as import receptors4,5,6,7 with a preference for preproteins that have amino-terminal presequences or internal targeting information, respectively. Tom40 is an essential constituent of the GIP8,9, whereas Tom6 and Tom7 modulate the assembly and dissociation of the Tom machinery10,11. Here we report the identification of Tom5, a small subunit that has a crucial role importing preproteins destined for all four mitochondrial subcompartments. Tom5 has a single membrane anchor and a cytosolic segment with a negative net charge, and accepts preproteins from the receptors and mediates their insertion into the GIP. We conclude that Tom5 represents a functional link between surface receptors and GIP, and is part of an ‘acid chain’5 that guides the stepwise transport of positively charged mitochondrial targeting sequences.

Suggested Citation

  • Klaus Dietmeier & Angelika Hönlinger & Ulf Bömer & Peter J. T. Dekker & Christoph Eckerskorn & Fritz Lottspeich & Michael Kübrich & Nikolaus Pfanner, 1997. "Tom5 functionally links mitochondrial preprotein receptors to the general import pore," Nature, Nature, vol. 388(6638), pages 195-200, July.
    • Handle: RePEc:nat:nature:v:388:y:1997:i:6638:d:10.1038_40663
    DOI: 10.1038/40663
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