Abstract
Insertion of beta-barrel proteins into the outer membrane of mitochondria is mediated by the TOB complex. Known constituents of this complex are Tob55 and Mas37. We identified a novel component, Tob38. It is essential for viability of yeast and the function of the TOB complex. Tob38 is exposed on the surface of the mitochondrial outer membrane. It interacts with Mas37 and Tob55 and is associated with Tob55 even in the absence of Mas37. The Tob38-Tob55 core complex binds precursors of beta-barrel proteins and facilitates their insertion into the outer membrane. Depletion of Tob38 results in strongly reduced levels of Tob55 and Mas37 and the residual proteins no longer form a complex. Tob38-depleted mitochondria are deficient in the import of beta-barrel precursor proteins, but not of other outer membrane proteins or proteins of other mitochondrial subcompartments. We conclude that Tob38 has a crucial function in the biogenesis of beta-barrel proteins of mitochondria.
MeSH Terms
Cell Membrane/metabolism
Cell Proliferation
DNA/metabolism
Detergents/pharmacology
Dose-Response Relationship, Drug
Down-Regulation
Electrophoresis, Polyacrylamide Gel
Escherichia coli/metabolism
Membrane Proteins/metabolism
Mitochondria/metabolism
Mitochondrial Proteins/chemistry,metabolism,physiology
Open Reading Frames
Protein Binding
Protein Structure, Secondary
Protein Structure, Tertiary
Saccharomyces cerevisiae/metabolism
Saccharomyces cerevisiae Proteins/chemistry,metabolism,physiology
Subcellular Fractions/metabolism
Time Factors
Chemicals
Detergents
Membrane Proteins
Mitochondrial Proteins
SAM37 protein, S cerevisiae
Saccharomyces cerevisiae Proteins
Sam35 protein, S cerevisiae
Sam50 protein, S cerevisiae
DNA
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Waizenegger Thomas
Institut für Physiologische Chemie der Universität München, Butenandtstrasse 5, Haus B, 81377 Munich, Germany.
Habib Shukry J
Lech Maciej
Mokranjac Dejana
Paschen Stefan A
Hell Kai
Neupert Walter
Rapaport Doron
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