Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 35, Issue 18, Pages 3200-3211Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.00107-15
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Funding
- Deutsche Forschungsgemeinschaft [RA 1048/5-1, RA 1048/7-1]
- PROMOS program of the DAAD
- Minerva grant
- European Research Council (ERC) starting grant (StG) [260395]
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A special group of mitochondrial outer membrane (MOM) proteins spans the membrane several times via multiple helical segments. Such multispan proteins are synthesized on cytosolic ribosomes before their targeting to mitochondria and insertion into the MOM. Previous work recognized the import receptor Tom70 and the mitochondrial import (MIM) complex, both residents of the MOM, as required for optimal biogenesis of these proteins. However, their involvement is not sufficient to explain either the entire import pathway or its regulation. To identify additional factors that are involved in the biogenesis ofMOMmultispan proteins, we performed complementary high-throughput visual and growth screens in Saccharomyces cerevisiae. Cardiolipin (CL) synthase (Crd1) appeared as a candidate in both screens. Our results indeed demonstrate lower steady-state levels of the multispan proteins Ugo1, Scm4, and Om14 in mitochondria from crd1 Delta cells. Importantly, MOMsingle-span proteins were not affected by this mutation. Furthermore, organelles lacking Crd1 had a lower in vitro capacity to import newly synthesized Ugo1 and Scm4 molecules. Crd1, which is located in the mitochondrial inner membrane, condenses phosphatidylglycerol together with CDP-diacylglycerol to obtain de novo synthesized CL molecules. Hence, our findings suggest that CL is an important component in the biogenesis ofMOMmultispan proteins.
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