Pfanner N

References (1)

Title : Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins - Zahedi_2006_Mol.Biol.Cell_17_1436
Author(s) : Zahedi RP , Sickmann A , Boehm AM , Winkler C , Zufall N , Schonfisch B , Guiard B , Pfanner N , Meisinger C
Ref : Mol Biology of the cell , 17 :1436 , 2006
Abstract : 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 Sjogren-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.
ESTHER : Zahedi_2006_Mol.Biol.Cell_17_1436
PubMedSearch : Zahedi_2006_Mol.Biol.Cell_17_1436
PubMedID: 16407407
Gene_locus related to this paper: yeast-mgll