Tom5 functionally links mitochondrial preprotein receptors to the general import pore

Klaus Dietmeier, Angelika Hönlinger, Ulf Bömer, Peter J. T. Dekker, Christoph Eckerskorn, Fritz Lottspeich, Michael Kübrich and Nikolaus Pfanner ()
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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

Nature, 1997, vol. 388, issue 6638, 195-200

Abstract: 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.

Date: 1997
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DOI: 10.1038/40663

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