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Proteomic profiling of the mitochondrial ribosome identifies Atp25 as a composite mitochondrial precursor protein
Whereas the structure and function of cytosolic ribosomes are well characterized, we only have a limited understanding of the mitochondrial translation apparatus. Using SILAC-based proteomic profiling, we identified 13 proteins that cofractionated with the mitochondrial ribosome, most of which play...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5063612/ https://www.ncbi.nlm.nih.gov/pubmed/27582385 http://dx.doi.org/10.1091/mbc.E16-07-0513 |
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author | Woellhaf, Michael W. Sommer, Frederik Schroda, Michael Herrmann, Johannes M. |
author_facet | Woellhaf, Michael W. Sommer, Frederik Schroda, Michael Herrmann, Johannes M. |
author_sort | Woellhaf, Michael W. |
collection | PubMed |
description | Whereas the structure and function of cytosolic ribosomes are well characterized, we only have a limited understanding of the mitochondrial translation apparatus. Using SILAC-based proteomic profiling, we identified 13 proteins that cofractionated with the mitochondrial ribosome, most of which play a role in translation or ribosomal biogenesis. One of these proteins is a homologue of the bacterial ribosome-silencing factor (Rsf). This protein is generated from the composite precursor protein Atp25 upon internal cleavage by the matrix processing peptidase MPP, and in this respect, it differs from all other characterized mitochondrial proteins of baker’s yeast. We observed that cytosolic expression of Rsf, but not of noncleaved Atp25 protein, is toxic. Our results suggest that eukaryotic cells face the challenge of avoiding negative interference from the biogenesis of their two distinct translation machineries. |
format | Online Article Text |
id | pubmed-5063612 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-50636122016-12-30 Proteomic profiling of the mitochondrial ribosome identifies Atp25 as a composite mitochondrial precursor protein Woellhaf, Michael W. Sommer, Frederik Schroda, Michael Herrmann, Johannes M. Mol Biol Cell Articles Whereas the structure and function of cytosolic ribosomes are well characterized, we only have a limited understanding of the mitochondrial translation apparatus. Using SILAC-based proteomic profiling, we identified 13 proteins that cofractionated with the mitochondrial ribosome, most of which play a role in translation or ribosomal biogenesis. One of these proteins is a homologue of the bacterial ribosome-silencing factor (Rsf). This protein is generated from the composite precursor protein Atp25 upon internal cleavage by the matrix processing peptidase MPP, and in this respect, it differs from all other characterized mitochondrial proteins of baker’s yeast. We observed that cytosolic expression of Rsf, but not of noncleaved Atp25 protein, is toxic. Our results suggest that eukaryotic cells face the challenge of avoiding negative interference from the biogenesis of their two distinct translation machineries. The American Society for Cell Biology 2016-10-15 /pmc/articles/PMC5063612/ /pubmed/27582385 http://dx.doi.org/10.1091/mbc.E16-07-0513 Text en © 2016 Woellhaf 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 for Cell Biology. |
spellingShingle | Articles Woellhaf, Michael W. Sommer, Frederik Schroda, Michael Herrmann, Johannes M. Proteomic profiling of the mitochondrial ribosome identifies Atp25 as a composite mitochondrial precursor protein |
title | Proteomic profiling of the mitochondrial ribosome identifies Atp25 as a composite mitochondrial precursor protein |
title_full | Proteomic profiling of the mitochondrial ribosome identifies Atp25 as a composite mitochondrial precursor protein |
title_fullStr | Proteomic profiling of the mitochondrial ribosome identifies Atp25 as a composite mitochondrial precursor protein |
title_full_unstemmed | Proteomic profiling of the mitochondrial ribosome identifies Atp25 as a composite mitochondrial precursor protein |
title_short | Proteomic profiling of the mitochondrial ribosome identifies Atp25 as a composite mitochondrial precursor protein |
title_sort | proteomic profiling of the mitochondrial ribosome identifies atp25 as a composite mitochondrial precursor protein |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5063612/ https://www.ncbi.nlm.nih.gov/pubmed/27582385 http://dx.doi.org/10.1091/mbc.E16-07-0513 |
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