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The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates
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 investigated the distribution of budding yeast Oxa1 between the two subdomains of the...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3374748/ https://www.ncbi.nlm.nih.gov/pubmed/22513091 http://dx.doi.org/10.1091/mbc.E11-06-0538 |
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author | Stoldt, Stefan Wenzel, Dirk Hildenbeutel, Markus Wurm, Christian A. Herrmann, Johannes M. Jakobs, Stefan |
author_facet | Stoldt, Stefan Wenzel, Dirk Hildenbeutel, Markus Wurm, Christian A. Herrmann, Johannes M. Jakobs, Stefan |
author_sort | Stoldt, Stefan |
collection | PubMed |
description | 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 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 nonfermentable (respiratory) growth conditions, it is predominantly localized in the CM. The enrichment of Oxa1 in the CM requires mitochondrial translation; similarly, 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 toward 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. |
format | Online Article Text |
id | pubmed-3374748 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-33747482012-08-30 The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates Stoldt, Stefan Wenzel, Dirk Hildenbeutel, Markus Wurm, Christian A. Herrmann, Johannes M. Jakobs, Stefan Mol Biol Cell Articles 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 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 nonfermentable (respiratory) growth conditions, it is predominantly localized in the CM. The enrichment of Oxa1 in the CM requires mitochondrial translation; similarly, 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 toward 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. The American Society for Cell Biology 2012-06-15 /pmc/articles/PMC3374748/ /pubmed/22513091 http://dx.doi.org/10.1091/mbc.E11-06-0538 Text en © 2012 Stoldt et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Stoldt, Stefan Wenzel, Dirk Hildenbeutel, Markus Wurm, Christian A. Herrmann, Johannes M. Jakobs, Stefan The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates |
title | The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates |
title_full | The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates |
title_fullStr | The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates |
title_full_unstemmed | The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates |
title_short | The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates |
title_sort | inner-mitochondrial distribution of oxa1 depends on the growth conditions and on the availability of substrates |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3374748/ https://www.ncbi.nlm.nih.gov/pubmed/22513091 http://dx.doi.org/10.1091/mbc.E11-06-0538 |
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