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Zahedi RP, et al.  (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol Biol Cell 17(3):1436-50

Abstract: 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 approximately 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 Sjogren-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.

Status: Published Type: Journal Article PubMed ID: 16407407

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