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 yea...
| Main Authors: | , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
BioMed Central
2010
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| _version_ | 1826289856965246976 |
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| author | Helbig, A Rosati, S Pijnappel, P van Breukelen, B Timmers, M Mohammed, S Slijper, M Heck, A |
| author_facet | Helbig, A Rosati, S Pijnappel, P van Breukelen, B Timmers, M Mohammed, S Slijper, M Heck, A |
| author_sort | Helbig, A |
| collection | OXFORD |
| 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 15N 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. |
| first_indexed | 2024-03-07T02:35:18Z |
| format | Journal article |
| id | oxford-uuid:a8947138-899c-49e8-825d-d8be060399be |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T02:35:18Z |
| publishDate | 2010 |
| publisher | BioMed Central |
| record_format | dspace |
| spelling | oxford-uuid:a8947138-899c-49e8-825d-d8be060399be2022-03-27T03:02:32ZPerturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:a8947138-899c-49e8-825d-d8be060399beEnglishSymplectic Elements at OxfordBioMed Central2010Helbig, ARosati, SPijnappel, Pvan Breukelen, BTimmers, MMohammed, SSlijper, MHeck, A 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 15N 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. |
| spellingShingle | Helbig, A Rosati, S Pijnappel, P van Breukelen, B Timmers, M Mohammed, S Slijper, M Heck, A 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 |
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