The inner-mitochondrial distribution of Oxa1 depends on the growth conditions 
and on the availability of substrates.

Stoldt, S.; Wenzel, D.; Hildenbeutel, M.; Wurm, C. A.; Hermann, J. M.; Jakobs, S.

doi:10.1091/mbc.E11-06-0538

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The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates.

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Stoldt, S.
Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Wenzel, D.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

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Wurm, C. A.
Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society;

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Jakobs, S.
Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Citation

Stoldt, S., Wenzel, D., Hildenbeutel, M., Wurm, C. A., Hermann, J. M., & Jakobs, S. (2012). The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates. Molecular Biology of the Cell, 23(12), 2292-2301. doi:10.1091/mbc.E11-06-0538.

Cite as: https://hdl.handle.net/11858/00-001M-0000-000F-9CFF-B

Abstract

The Oxa1 protein is a well-conserved integral protein of the inner membrane of mitochondria. It mediates the insertion of both mitochondrial- and nuclear-encoded proteins from the matrix into the inner membrane. We have investigated the distribution of budding yeast Oxa1 between the two subdomains of the contiguous inner membrane, the cristae membrane (CM) and the inner boundary membrane (IBM), under different physiological conditions. We found that under fermentable growth conditions, Oxa1 is enriched in the IBM, whereas under non-fermentable (respiratory) growth conditions, it is predominantly localized in the CM. The enrichment of Oxa1 in the CM requires mitochondrial translation; likewise, deletion of the ribosome binding domain of Oxa1 prevents an enrichment of Oxa1 in the CM. The predominant localization in the IBM under fermentable growth conditions is prevented by inhibiting mitochondrial protein import. Furthermore, overexpression of the nuclear-encoded Oxa1 substrate Mdl1 shifts the distribution of Oxa1 towards the IBM. Apparently, the availability of nuclear and mitochondrial-encoded substrates influences the inner-membrane distribution of Oxa1. Our findings show that the distribution of Oxa1 within the inner membrane is dynamic and adapts to different physiological needs.