Abstract

The mitochondrial inner membrane is rich in multispanning integral membrane proteins, most of which mediate the vital transport of molecules between the matrix and the intermembrane space. The correct transport and membrane insertion of such proteins is essential for maintaining the correct exchange of molecules between mitochondria and the rest of the cell. Mitochondria contain several specific complexes — known as translocases — that translocate precursor proteins. Recent analysis of the inner-membrane, twin-pore protein translocase (TIM22 complex) allows a glimpse of the molecular mechanisms by which this machinery triggers protein insertion using the membrane potential as an external driving force.

Author affiliations

1. Institut für Biochemie und Molekularbiologie, Universität Freiburg, Hermann-Herder-Strae 7, D-79104 Freiburg, Germany.

Correspondence to: Peter Rehling¹ Email: peter.rehling@biochemie.uni-freiburg.de

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