Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast

Lyris M. F. de Godoy, Jesper V. Olsen, Jürgen Cox, Michael L. Nielsen, Nina C. Hubner, Florian Fröhlich, Tobias C. Walther () and Matthias Mann ()
Additional contact information
Lyris M. F. de Godoy: Proteomics and Signal Transduction, and,
Jesper V. Olsen: Proteomics and Signal Transduction, and,
Jürgen Cox: Proteomics and Signal Transduction, and,
Michael L. Nielsen: Proteomics and Signal Transduction, and,
Nina C. Hubner: Proteomics and Signal Transduction, and,
Florian Fröhlich: Organelle Architecture and Dynamics, Max-Planck-Institute for Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany
Tobias C. Walther: Organelle Architecture and Dynamics, Max-Planck-Institute for Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany
Matthias Mann: Proteomics and Signal Transduction, and,

Nature, 2008, vol. 455, issue 7217, 1251-1254

Abstract: The yeast proteome quantified A combination of high-resolution mass spectrometry, 'SILAC' labelling and computational proteomics has been used to achieve an important goal in proteomics: the complete identification and quantification of a proteome. The analysis reveals a proteome made up of 4,399 individual endogenous proteins, essentially the complete proteome in terms of proteins expressed in normally growing yeast cells. The levels of these proteins in haploid cells were compared to the levels in diploid cells. Among other differences, cell wall components are significantly down-regulated in diploids — in line with the fact that diploid cells are twice as large as haploid cells but do not have twice the surface area.

Date: 2008
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DOI: 10.1038/nature07341

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