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A Deubiquitylating Complex Required for Neosynthesis of a Yeast Mitochondrial ATP Synthase Subunit
The ubiquitin system is known to be involved in maintaining the integrity of mitochondria, but little is known about the role of deubiquitylating (DUB) enzymes in such functions. Budding yeast cells deleted for UBP13 and its close homolog UBP9 displayed a high incidence of petite colonies and slow r...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3378586/ https://www.ncbi.nlm.nih.gov/pubmed/22723847 http://dx.doi.org/10.1371/journal.pone.0038071 |
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author | Kanga, Sophie Bernard, Delphine Mager-Heckel, Anne-Marie Erpapazoglou, Zoi Mattiroli, Francesca Sixma, Titia K. Léon, Sébastien Urban-Grimal, Danièle Tarassov, Ivan Haguenauer-Tsapis, Rosine |
author_facet | Kanga, Sophie Bernard, Delphine Mager-Heckel, Anne-Marie Erpapazoglou, Zoi Mattiroli, Francesca Sixma, Titia K. Léon, Sébastien Urban-Grimal, Danièle Tarassov, Ivan Haguenauer-Tsapis, Rosine |
author_sort | Kanga, Sophie |
collection | PubMed |
description | The ubiquitin system is known to be involved in maintaining the integrity of mitochondria, but little is known about the role of deubiquitylating (DUB) enzymes in such functions. Budding yeast cells deleted for UBP13 and its close homolog UBP9 displayed a high incidence of petite colonies and slow respiratory growth at 37°C. Both Ubp9 and Ubp13 interacted directly with Duf1 (DUB-associated factor 1), a WD40 motif-containing protein. Duf1 activates the DUB activity of recombinant Ubp9 and Ubp13 in vitro and deletion of DUF1 resulted in the same respiratory phenotype as the deletion of both UBP9 and UBP13. We show that the mitochondrial defects of these mutants resulted from a strong decrease at 37°C in the de novo biosynthesis of Atp9, a membrane-bound component of ATP synthase encoded by mitochondrial DNA. The defect appears at the level of ATP9 mRNA translation, while its maturation remained unchanged in the mutants. This study describes a new role of the ubiquitin system in mitochondrial biogenesis. |
format | Online Article Text |
id | pubmed-3378586 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-33785862012-06-21 A Deubiquitylating Complex Required for Neosynthesis of a Yeast Mitochondrial ATP Synthase Subunit Kanga, Sophie Bernard, Delphine Mager-Heckel, Anne-Marie Erpapazoglou, Zoi Mattiroli, Francesca Sixma, Titia K. Léon, Sébastien Urban-Grimal, Danièle Tarassov, Ivan Haguenauer-Tsapis, Rosine PLoS One Research Article The ubiquitin system is known to be involved in maintaining the integrity of mitochondria, but little is known about the role of deubiquitylating (DUB) enzymes in such functions. Budding yeast cells deleted for UBP13 and its close homolog UBP9 displayed a high incidence of petite colonies and slow respiratory growth at 37°C. Both Ubp9 and Ubp13 interacted directly with Duf1 (DUB-associated factor 1), a WD40 motif-containing protein. Duf1 activates the DUB activity of recombinant Ubp9 and Ubp13 in vitro and deletion of DUF1 resulted in the same respiratory phenotype as the deletion of both UBP9 and UBP13. We show that the mitochondrial defects of these mutants resulted from a strong decrease at 37°C in the de novo biosynthesis of Atp9, a membrane-bound component of ATP synthase encoded by mitochondrial DNA. The defect appears at the level of ATP9 mRNA translation, while its maturation remained unchanged in the mutants. This study describes a new role of the ubiquitin system in mitochondrial biogenesis. Public Library of Science 2012-06-19 /pmc/articles/PMC3378586/ /pubmed/22723847 http://dx.doi.org/10.1371/journal.pone.0038071 Text en Kanga et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Kanga, Sophie Bernard, Delphine Mager-Heckel, Anne-Marie Erpapazoglou, Zoi Mattiroli, Francesca Sixma, Titia K. Léon, Sébastien Urban-Grimal, Danièle Tarassov, Ivan Haguenauer-Tsapis, Rosine A Deubiquitylating Complex Required for Neosynthesis of a Yeast Mitochondrial ATP Synthase Subunit |
title | A Deubiquitylating Complex Required for Neosynthesis of a Yeast Mitochondrial ATP Synthase Subunit |
title_full | A Deubiquitylating Complex Required for Neosynthesis of a Yeast Mitochondrial ATP Synthase Subunit |
title_fullStr | A Deubiquitylating Complex Required for Neosynthesis of a Yeast Mitochondrial ATP Synthase Subunit |
title_full_unstemmed | A Deubiquitylating Complex Required for Neosynthesis of a Yeast Mitochondrial ATP Synthase Subunit |
title_short | A Deubiquitylating Complex Required for Neosynthesis of a Yeast Mitochondrial ATP Synthase Subunit |
title_sort | deubiquitylating complex required for neosynthesis of a yeast mitochondrial atp synthase subunit |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3378586/ https://www.ncbi.nlm.nih.gov/pubmed/22723847 http://dx.doi.org/10.1371/journal.pone.0038071 |
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