Open Access Research article

Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels

Andreas O Helbig12, Sara Rosati12, Pim WWM Pijnappel23, Bas van Breukelen125, Marc HTH Timmers23, Shabaz Mohammed12, Monique Slijper12 and Albert JR Heck124*

Author Affiliations

1 Biomolecular Mass Spectrometry and Proteomics Group, Utrecht Institute for Pharmaceutical Sciences and Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, Utrecht, 3584 CH, The Netherlands

2 Netherlands Proteomics Centre, Padualaan 8, Utrecht, 3584 CH, The Netherlands

3 University Medical Center Utrecht, Universiteitsweg 100, Utrecht, 3584 CG, The Netherlands

4 Center for Biomedical Genetics, MCU, Stratenum 3.223, Universiteitsweg 100, Utrecht, 3584 CG, The Netherlands

5 Netherlands Bioinformatics Centre, Geert Grooteplein 28, Nijmgen, 6525 GA, The Netherlands

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BMC Genomics 2010, 11:685  doi:10.1186/1471-2164-11-685

Published: 2 December 2010

Additional files

Additional file 1:

Table S1. N-acetylation. displays an inventory of acetylated protein N-termini in S. cerevisiae.

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Additional file 2:

Table S2. Protein levels. displays 15N/14N isotopic ratios of protein levels comparing WT and nat3Δ.

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Additional file 3:

Table S3. Posphorylated peptides. displays quantified phosphorylated peptides from the WT and nat3Δ.

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Additional file 4:

Table S4. NatB substrates. displays an inventory of detected NatB substrates.

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Additional file 5:

Table S5. Protein variants. displays an inventory of detected protein variants.

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Additional file 6:

Table S6. In-silico digestion. shows detectable N-terminal peptides after in-silico digestion using trypsin or Lys-N.

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