The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry
Open accessAbstract
We present a strategy for the analysis of the yeast phosphoproteome that uses endo-Lys C as the proteolytic enzyme, immobilized metal affinity chromatography for phosphopeptide enrichment, a 90-min nanoflow-HPLC/electrospray-ionization MS/MS experiment for phosphopeptide fractionation and detection, gas phase ion/ion chemistry, electron transfer dissociation for peptide fragmentation, and the Open Mass Spectrometry Search Algorithm for phosphoprotein identification and assignment of phosphorylation sites. From a 30-μg (≈600 pmol) sample of total yeast protein, we identify 1,252 phosphorylation sites on 629 proteins. Identified phosphoproteins have expression levels that range from <50 to 1,200,000 copies per cell and are encoded by genes involved in a wide variety of cellular processes. We identify a consensus site that likely represents a motif for one or more uncharacterized kinases and show that yeast kinases, themselves, contain a disproportionately large number of phosphorylation sites. Detection of a pHis containing peptide from the yeast protein, Cdc10, suggests an unexpected role for histidine phosphorylation in septin biology. From diverse functional genomics data, we show that phosphoproteins have a higher number of interactions than an average protein and interact with each other more than with a random protein. They are also likely to be conserved across large evolutionary distances.
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Cites
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Self-citationPhosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae
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Cited by
Protein Analysis by Shotgun/Bottom-up Proteomics
Zhang, Y., Fonslow, B. R., Shan, B., Baek, M.-C., & Yates, J. R. (2013) · Chemical Reviews · doi:10.1021/cr3003533 · Cited by 1,491
Proteomics by Mass Spectrometry: Approaches, Advances, and Applications
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A Global Protein Kinase and Phosphatase Interaction Network in Yeast
Breitkreutz, A., Choi, H., Sharom, J. R., Boucher, L., Neduva, V., Larsen, B., Lin, Z.-Y., Breitkreutz, B.-J., Stark, C., Liu, G., et al. (2010) · Science · doi:10.1126/science.1176495 · Cited by 683
The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry
Villén, J., & Gygi, S. P. (2008) · Nature Protocols · doi:10.1038/nprot.2008.150 · Cited by 629
A Multidimensional Chromatography Technology for In-depth Phosphoproteome Analysis
Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., & Zhou, H. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700468-mcp200 · Cited by 504
Metadata
- Authors
- Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E. P., Bai, D. L., Shabanowitz, J., Burke, D. J., Troyanskaya, O. G., & Hunt, D. F.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2007-02-13
- Volume
- 104
- Issue
- 7
- Pages
- 2193-2198
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2090806203
- Cited by
- 564
- References
- 34
- FWCI
- 32.39
- Type
- journal article
- Language
- en
- Open access
- green
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- Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E. P., Bai, D. L., Shabanowitz, J., Burke, D. J., Troyanskaya, O. G., & Hunt, D. F. (2007). Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0607084104
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