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Comprehensive quantitative analysis of central carbon and amino-acid metabolism in Saccharomyces cerevisiae under multiple conditions by targeted proteomics
Decades of biochemical research have identified most of the enzymes that catalyze metabolic reactions in the yeast Saccharomyces cerevisiae. The adaptation of metabolism to changing nutritional conditions, in contrast, is much less well understood. As an important stepping stone toward such understa...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
European Molecular Biology Organization
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3063691/ https://www.ncbi.nlm.nih.gov/pubmed/21283140 http://dx.doi.org/10.1038/msb.2010.122 |
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author | Costenoble, Roeland Picotti, Paola Reiter, Lukas Stallmach, Robert Heinemann, Matthias Sauer, Uwe Aebersold, Ruedi |
author_facet | Costenoble, Roeland Picotti, Paola Reiter, Lukas Stallmach, Robert Heinemann, Matthias Sauer, Uwe Aebersold, Ruedi |
author_sort | Costenoble, Roeland |
collection | PubMed |
description | Decades of biochemical research have identified most of the enzymes that catalyze metabolic reactions in the yeast Saccharomyces cerevisiae. The adaptation of metabolism to changing nutritional conditions, in contrast, is much less well understood. As an important stepping stone toward such understanding, we exploit the power of proteomics assays based on selected reaction monitoring (SRM) mass spectrometry to quantify abundance changes of the 228 proteins that constitute the central carbon and amino-acid metabolic network in the yeast Saccharomyces cerevisiae, at five different metabolic steady states. Overall, 90% of the targeted proteins, including families of isoenzymes, were consistently detected and quantified in each sample, generating a proteomic data set that represents a nutritionally perturbed biological system at high reproducibility. The data set is near comprehensive because we detect 95–99% of all proteins that are required under a given condition. Interpreted through flux balance modeling, the data indicate that S. cerevisiae retains proteins not necessarily used in a particular environment. Further, the data suggest differential functionality for several metabolic isoenzymes. |
format | Text |
id | pubmed-3063691 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | European Molecular Biology Organization |
record_format | MEDLINE/PubMed |
spelling | pubmed-30636912011-03-25 Comprehensive quantitative analysis of central carbon and amino-acid metabolism in Saccharomyces cerevisiae under multiple conditions by targeted proteomics Costenoble, Roeland Picotti, Paola Reiter, Lukas Stallmach, Robert Heinemann, Matthias Sauer, Uwe Aebersold, Ruedi Mol Syst Biol Article Decades of biochemical research have identified most of the enzymes that catalyze metabolic reactions in the yeast Saccharomyces cerevisiae. The adaptation of metabolism to changing nutritional conditions, in contrast, is much less well understood. As an important stepping stone toward such understanding, we exploit the power of proteomics assays based on selected reaction monitoring (SRM) mass spectrometry to quantify abundance changes of the 228 proteins that constitute the central carbon and amino-acid metabolic network in the yeast Saccharomyces cerevisiae, at five different metabolic steady states. Overall, 90% of the targeted proteins, including families of isoenzymes, were consistently detected and quantified in each sample, generating a proteomic data set that represents a nutritionally perturbed biological system at high reproducibility. The data set is near comprehensive because we detect 95–99% of all proteins that are required under a given condition. Interpreted through flux balance modeling, the data indicate that S. cerevisiae retains proteins not necessarily used in a particular environment. Further, the data suggest differential functionality for several metabolic isoenzymes. European Molecular Biology Organization 2011-02-01 /pmc/articles/PMC3063691/ /pubmed/21283140 http://dx.doi.org/10.1038/msb.2010.122 Text en Copyright © 2011, EMBO and Macmillan Publishers Limited https://creativecommons.org/licenses/by-nc-sa/3.0/This is an open-access article distributed under the terms of the Creative Commons Attribution Noncommercial Share Alike 3.0 Unported License, which allows readers to alter, transform, or build upon the article and then distribute the resulting work under the same or similar license to this one. The work must be attributed back to the original author and commercial use is not permitted without specific permission. |
spellingShingle | Article Costenoble, Roeland Picotti, Paola Reiter, Lukas Stallmach, Robert Heinemann, Matthias Sauer, Uwe Aebersold, Ruedi Comprehensive quantitative analysis of central carbon and amino-acid metabolism in Saccharomyces cerevisiae under multiple conditions by targeted proteomics |
title | Comprehensive quantitative analysis of central carbon and amino-acid metabolism in Saccharomyces cerevisiae under multiple conditions by targeted proteomics |
title_full | Comprehensive quantitative analysis of central carbon and amino-acid metabolism in Saccharomyces cerevisiae under multiple conditions by targeted proteomics |
title_fullStr | Comprehensive quantitative analysis of central carbon and amino-acid metabolism in Saccharomyces cerevisiae under multiple conditions by targeted proteomics |
title_full_unstemmed | Comprehensive quantitative analysis of central carbon and amino-acid metabolism in Saccharomyces cerevisiae under multiple conditions by targeted proteomics |
title_short | Comprehensive quantitative analysis of central carbon and amino-acid metabolism in Saccharomyces cerevisiae under multiple conditions by targeted proteomics |
title_sort | comprehensive quantitative analysis of central carbon and amino-acid metabolism in saccharomyces cerevisiae under multiple conditions by targeted proteomics |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3063691/ https://www.ncbi.nlm.nih.gov/pubmed/21283140 http://dx.doi.org/10.1038/msb.2010.122 |
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