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Originally published In Press as doi:10.1074/mcp.M300081-MCP200 on November 15, 2003.
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Molecular & Cellular Proteomics 3:125-132, 2004.
© 2004 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

A Comparative Analysis of an Orthologous Proteomic Environment in the Yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe*,S

Assen Roguev{ddagger},§, Anna Shevchenko§,¶, Daniel Schaft{ddagger}, Henrik Thomas, A. Francis Stewart{ddagger},|| and Andrej Shevchenko,||

From {ddagger} Genomics, Technische Universität Dresden, c/o Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany; and Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany

The sequential application of protein tagging, affinity purification, and mass spectrometry enables highly accurate charting of proteomic environments by the characterization of stable protein assemblies and the identification of subunits that are shared between two or more protein complexes, termed here "proteomic hyperlinks." We have charted the proteomic environments surrounding the histone methyltransferase, Set1, in both yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. Although the composition of these nonessential Set1 complexes is remarkably conserved, they differ with respect to their hyperlinks to their proteomic environments. We speculate that conservation of the core components of protein assemblies and variability of hyperlinks represents a general principle in the molecular organization of eukaryotic proteomes.

|| To whom correspondence should be addressed. E-mail: shevchenko{at}mpi-cbg.de and stewart{at}mpi-cbg.de


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