scholarly journals Characterization of a novel β-barrel protein (AtOM47) from the mitochondrial outer membrane ofArabidopsis thaliana

2016 ◽  
Vol 67 (21) ◽  
pp. 6061-6075 ◽  
Author(s):  
Lu Li ◽  
Szymon Kubiszewski-Jakubiak ◽  
Jordan Radomiljac ◽  
Yan Wang ◽  
Simon R. Law ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Mitochondrial Outer Membrane ◽  
Ofarabidopsis Thaliana

Further Characterization of Mitochondrial Outer Membrane: Evidence for the Presence of Two Endogenous Sialylated Glycoproteins1

1994 ◽  
Vol 116 (3) ◽  
pp. 643-648 ◽  
Author(s):  
Françcoise Gasnier ◽  
Dominique Ardail ◽  
Fabienne Lermé ◽  
Cédric Simonot ◽  
Elisabeth Vaganay ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Mitochondrial Outer Membrane

scholarly journals Characterization of the signal that directs Bcl-xL, but not Bcl-2, to the mitochondrial outer membrane

2003 ◽  
Vol 160 (1) ◽  
pp. 53-64 ◽  
Author(s):  
Thomas Kaufmann ◽  
Sarah Schlipf ◽  
Javier Sanz ◽  
Karin Neubert ◽  
Reuven Stein ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Mitochondrial Outer Membrane ◽  
Mitochondrial Targeting ◽  
Mitochondrial Localization ◽  
Intracellular Membranes ◽  
Bona Fide ◽  
Targeting Signal ◽  
Tm Domain ◽  
Mitochondrial Targeting Sequences

It is assumed that the survival factors Bcl-2 and Bcl-xL are mainly functional on mitochondria and therefore must contain mitochondrial targeting sequences. Here we show, however, that only Bcl-xL is specifically targeted to the mitochondrial outer membrane (MOM) whereas Bcl-2 distributes on several intracellular membranes. Mitochondrial targeting of Bcl-xL requires the COOH-terminal transmembrane (TM) domain flanked at both ends by at least two basic amino acids. This sequence is a bona fide targeting signal for the MOM as it confers specific mitochondrial localization to soluble EGFP. The signal is present in numerous proteins known to be directed to the MOM. Bcl-2 lacks the signal and therefore localizes to several intracellular membranes. The COOH-terminal region of Bcl-2 can be converted into a targeting signal for the MOM by increasing the basicity surrounding its TM. These data define a new targeting sequence for the MOM and propose that Bcl-2 acts on several intracellular membranes whereas Bcl-xL specifically functions on the MOM.

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

2006 ◽  
Vol 17 (3) ◽  
pp. 1436-1450 ◽  
Author(s):  
Rene P. Zahedi ◽  
Albert Sickmann ◽  
Andreas M. Boehm ◽  
Christiane Winkler ◽  
Nicole Zufall ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Matrix Protein ◽  
Outer Membrane Proteins ◽  
Model Organism ◽  
Mitochondrial Outer Membrane ◽  
Intermembrane Space ◽  
Yeast Saccharomyces Cerevisiae ◽  
Cellular Processes ◽  
Genome Wide

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 ∼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 Sjögren–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.

scholarly journals Characterization of Rat TOM40, a Central Component of the Preprotein Translocase of the Mitochondrial Outer Membrane

2000 ◽  
Vol 275 (48) ◽  
pp. 37930-37936 ◽  
Author(s):  
Hiroyuki Suzuki ◽  
Yoshikazu Okazawa ◽  
Tohru Komiya ◽  
Kazuko Saeki ◽  
Eisuke Mekada ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Mitochondrial Outer Membrane ◽  
Central Component
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