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- Title
Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels.
- Authors
Helbig, Andreas O.; Rosati, Sara; Pijnappel, Pim W. W. M.; van Breukelen, Bas; Timmers, Marc H. T. H.; Mohammed, Shabaz; Slijper, Monique; Heck, Albert J. R.
- Abstract
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 nonannotated 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.
- Subjects
YEAST; ACETYLTRANSFERASES; PHOSPHORYLATION; ACYLTRANSFERASES; PROTEOMICS
- Publication
BMC Genomics, 2010, Vol 11, p685
- ISSN
1471-2164
- Publication type
Article
- DOI
10.1186/1471-2164-11-685