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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...

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Autores principales: Woellhaf, Michael W., Sommer, Frederik, Schroda, Michael, Herrmann, Johannes M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2016
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.
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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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