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Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels
BACKGROUND: The addition of an acetyl group to protein N-termini is a widespread co-translational modification. NatB is one of the main N-acetyltransferases that targets a subset of proteins possessing an N-terminal methionine, but so far only a handful of substrates have been reported. Using a yeas...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3091791/ https://www.ncbi.nlm.nih.gov/pubmed/21126336 http://dx.doi.org/10.1186/1471-2164-11-685 |
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author | Helbig, Andreas O Rosati, Sara Pijnappel, Pim WWM van Breukelen, Bas Timmers, Marc HTH Mohammed, Shabaz Slijper, Monique Heck, Albert JR |
author_facet | Helbig, Andreas O Rosati, Sara Pijnappel, Pim WWM van Breukelen, Bas Timmers, Marc HTH Mohammed, Shabaz Slijper, Monique Heck, Albert JR |
author_sort | Helbig, Andreas O |
collection | PubMed |
description | BACKGROUND: The addition of an acetyl group to protein N-termini is a widespread co-translational modification. NatB is one of the main N-acetyltransferases that targets a subset of proteins possessing an N-terminal methionine, but so far only a handful of substrates have been reported. Using a yeast nat3Δ strain, deficient for the catalytic subunit of NatB, we employed a quantitative proteomics strategy to identify NatB substrates and to characterize downstream effects in nat3Δ. RESULTS: Comparing by proteomics WT and nat3Δ strains, using metabolic (15)N isotope labeling, we confidently identified 59 NatB substrates, out of a total of 756 detected acetylated protein N-termini. We acquired in-depth proteome wide measurements of expression levels of about 2580 proteins. Most remarkably, NatB deletion led to a very significant change in protein phosphorylation. CONCLUSIONS: Protein expression levels change only marginally in between WT and nat3Δ. A comparison of the detected NatB substrates with their orthologous revealed remarkably little conservation throughout the phylogenetic tree. We further present evidence of post-translational N-acetylation on protein variants at non-annotated N-termini. Moreover, analysis of downstream effects in nat3Δ revealed elevated protein phosphorylation levels whereby the kinase Snf1p is likely a key element in this process. |
format | Text |
id | pubmed-3091791 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-30917912011-05-11 Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels Helbig, Andreas O Rosati, Sara Pijnappel, Pim WWM van Breukelen, Bas Timmers, Marc HTH Mohammed, Shabaz Slijper, Monique Heck, Albert JR BMC Genomics Research Article BACKGROUND: The addition of an acetyl group to protein N-termini is a widespread co-translational modification. NatB is one of the main N-acetyltransferases that targets a subset of proteins possessing an N-terminal methionine, but so far only a handful of substrates have been reported. Using a yeast nat3Δ strain, deficient for the catalytic subunit of NatB, we employed a quantitative proteomics strategy to identify NatB substrates and to characterize downstream effects in nat3Δ. RESULTS: Comparing by proteomics WT and nat3Δ strains, using metabolic (15)N isotope labeling, we confidently identified 59 NatB substrates, out of a total of 756 detected acetylated protein N-termini. We acquired in-depth proteome wide measurements of expression levels of about 2580 proteins. Most remarkably, NatB deletion led to a very significant change in protein phosphorylation. CONCLUSIONS: Protein expression levels change only marginally in between WT and nat3Δ. A comparison of the detected NatB substrates with their orthologous revealed remarkably little conservation throughout the phylogenetic tree. We further present evidence of post-translational N-acetylation on protein variants at non-annotated N-termini. Moreover, analysis of downstream effects in nat3Δ revealed elevated protein phosphorylation levels whereby the kinase Snf1p is likely a key element in this process. BioMed Central 2010-12-02 /pmc/articles/PMC3091791/ /pubmed/21126336 http://dx.doi.org/10.1186/1471-2164-11-685 Text en Copyright ©2010 Helbig et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Helbig, Andreas O Rosati, Sara Pijnappel, Pim WWM van Breukelen, Bas Timmers, Marc HTH Mohammed, Shabaz Slijper, Monique Heck, Albert JR Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels |
title | Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels |
title_full | Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels |
title_fullStr | Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels |
title_full_unstemmed | Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels |
title_short | Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels |
title_sort | perturbation of the yeast n-acetyltransferase natb induces elevation of protein phosphorylation levels |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3091791/ https://www.ncbi.nlm.nih.gov/pubmed/21126336 http://dx.doi.org/10.1186/1471-2164-11-685 |
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