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. 1999 Jul 26;146(2):321–332. doi: 10.1083/jcb.146.2.321

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© 1999 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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Working model of the insertion pathway of Tom40. Tom40 is presented to the mitochondria in a (partially) folded state and is initially recognized on the surface by the receptor Tom20. At this or a previous stage it is released in an ATP-dependent process from its interaction with cytosolic factors. The surface-bound Tom40 is only loosely attached to the TOM complex and after solubilization with mild detergent can be detected in monomeric state (M). In the next stage, initial insertion of the precursor into the translocation pore occurs (I). By this step the precursor acquires a state partially protected from externally added trypsin. The processes up to this point can take place rather efficiently also at 0°C. The next step, full assembly into the TOM complex (A), requires higher temperature and occurs when the NH₂ terminus of Tom40 is intact.