Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1827, Issue 5, Pages 612-626Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2012.12.004
Keywords
Inner membrane; Mitochondrion; Protein import; Respiratory chain; Succinate dehydrogenase
Categories
Funding
- Excellence Initiative of the German Federal Government [EXC 294 BIOSS]
- Excellence Initiative of the German State Government [EXC 294 BIOSS]
- Alexander von Humboldt-Foundation
- Deutsche Akademie der Naturforscher Leopoldina
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The mitochondrial inner membrane harbors the complexes of the respiratory chain and protein translocases required for the import of mitochondrial precursor proteins. These complexes are functionally interdependent, as the import of respiratory chain precursor proteins across and into the inner membrane requires the membrane potential. Vice versa the membrane potential is generated by the proton pumping complexes of the respiratory chain. Besides this basic codependency four different systems for protein import, processing and assembly show further connections to the respiratory chain. The mitochondrial intermembrane space import and assembly machinery oxidizes cysteine residues within the imported precursor proteins and is able to donate the liberated electrons to the respiratory chain. The presequence translocase of the inner membrane physically interacts with the respiratory chain. The mitochondrial processing peptidase is homologous to respiratory chain subunits and the carrier translocase of the inner membrane even shares a subunit with the respiratory chain. In this review we will summarize the import of mitochondrial precursor proteins and highlight these special links between the mitochondrial protein import machinery and the respiratory chain. This article is part of a Special Issue entitled: Respiratory complex Role in cellular physiology and disease. (C) 2012 Elsevier B.V. All rights reserved.
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