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MBC in Press, published online ahead of print January 11, 2006
Mol. Biol. Cell 10.1091/mbc.E05-08-0740

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Submitted on August 9, 2005
Revised on December 21, 2005
Accepted on January 3, 2006

Proteomic Analysis of the Yeast Mitochondrial Outer Membrane Reveals Accumulation of a Subclass of Preproteins

Rene P. Zahedi,* Albert Sickmann,* Andreas M. Boehm,* Christiane Winkler,* Nicole Zufall,{dagger} Birgit Schönfisch,{dagger} Bernard Guiard,{ddagger} Nikolaus Pfanner,{dagger} and Chris Meisinger{dagger}

*Rudolf-Virchow-Center for Experimental Biomedicine, Universität Würzburg, D-97078 Würzburg, Germany; {dagger}Institut für Biochemie und Molekularbiologie, Universität Freiburg, D-79104 Freiburg, Germany; {ddagger}Centre de Génétique Moléculaire, Laboratoire propre du CNRS, F-91190 Gif-sur-Yvette, France

Monitoring Editor: Benjamin Glick

Mitochondria consist of four compartments, outer membrane, intermembrane space, inner membrane and matrix, with crucial but distinct functions for numerous cellular processes. A comprehensive characterization of the proteome of an individual mitochondrial compartment has not been reported so far. We used a eukaryotic model organism, the yeast S. cerevisiae, to determine the proteome of highly purified mitochondrial outer membranes. We obtained a coverage of ~85% based on the known outer membrane proteins. The proteome represents a rich source for the analysis of new functions of the outer membrane, including the yeast homolog (Hfd1/Ymr110c) of the human protein causing Sjögren-Larsson syndrome. Surprisingly, a subclass of proteins known to reside in internal mitochondrial compartments were found in the outer membrane proteome. Those seemingly mislocalized proteins included most top scorers of a genome-wide analysis for mRNAs that were targeted to mitochondria and coded for proteins of prokaryotic origin (Marc et al., 2002, EMBO Rep. 3, 159). Together with the enrichment of the precursor form of a matrix protein in the outer membrane, we conclude that the mitochondrial outer membrane does not only contain resident proteins but also accumulates a conserved subclass of preproteins destined for internal mitochondrial compartments.

Address correspondence to: Albert Sickmann (Albert.Sickmann{at}virchow.uni-wuerzburg.de) or Chris Meisinger (Christof.Meisinger{at}biochemie.uni-freiburg.de)




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