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Published 12 September 2005. doi:10.1083/jcb.200505126
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 170, Number 6, 881-888
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 Proline residues of transmembrane domains determine the sorting of inner membrane proteins in mitochondria

Stephan Meier, Walter Neupert, and Johannes M. Herrmann

Institut für Physiologische Chemie, Universität München, 81377 München, Germany

Correspondence to Johannes Herrmann: hannes.herrmann{at}med.uni-muenchen.de


Abstract
Most inner membrane proteins of mitochondria are synthesized in the cytosol and reach the inner membrane using one of two alternative sorting pathways. On the stop transfer route, proteins are arrested during import at the level of the inner membrane. The conservative sorting pathway involves translocation through the inner membrane and insertion from the matrix. It is unclear how the translocase of the inner membrane 23 protein translocation machinery differentiates between the two classes of proteins. Here we show that proline residues in hydrophobic stretches strongly disfavor the translocation arrest of transmembrane domains (TMDs) and favor the transfer of preproteins to the matrix. We propose that proline residues, together with the hydrophobicity of the TMD and the presence of charged residues COOH-terminally flanking the TMD, are determinants of the intramitochondrial sorting of inner membrane proteins.

Abbreviations used in this paper: TIM, translocase of the inner membrane; TMD, transmembrane domain.


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