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Article Dans Une Revue Molecular Biology of the Cell Année : 2006

Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins.

Résumé

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 Saccharomyces 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 homologue (Hfd1/Ymr110c) of the human protein causing Sj?n-Larsson syndrome. Surprisingly, a subclass of proteins known to reside in internal mitochondrial compartments were found in the outer membrane proteome. These seemingly mislocalized proteins included most top scorers of a recent genome-wide analysis for mRNAs that were targeted to mitochondria and coded for proteins of prokaryotic origin. Together with the enrichment of the precursor form of a matrix protein in the outer membrane, we conclude that the mitochondrial outer membrane not only contains resident proteins but also accumulates a conserved subclass of preproteins destined for internal mitochondrial compartments.

Dates et versions

hal-00168063 , version 1 (24-08-2007)

Identifiants

Citer

Rene P Zahedi, Albert Sickmann, Andreas M Boehm, Christiane Winkler, Nicole Zufall, et al.. Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins.. Molecular Biology of the Cell, 2006, 17 (3), pp.1436-50. ⟨10.1091/mbc.E05-08-0740⟩. ⟨hal-00168063⟩
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