Research
Chromatin Central: towards the comparative proteome by accurate mapping of the yeast proteomic environment
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* Corresponding authors: Andrej Shevchenko shevchenko@mpi-cbg.de - A Francis Stewart stewart@biotec.tu-dresden.de
1 MPI of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany
2 Genomics, BioInnovationsZentrum, Technische Universität Dresden, Am Tatzberg 47-51, 01307 Dresden, Germany
3 Department of Cellular and Molecular Pharmacology, University of California, San Francisco, 1700 4th Street, San Francisco, CA 94158, USA
Genome Biology 2008, 9:R167 doi:10.1186/gb-2008-9-11-r167
Published: 28 November 2008Additional files
Additional data file 1:
Table S1: common background proteins observed in TAP experiments in S. cerevisiae and S. pombe. Table S2: full lists of proteins identified in all immunoprecipitation experiments in both yeasts. Tables S3: master table of identified proteins used for compiling Chromatin Central in S. cerevisiae. Table S4 master table of identified proteins used for compiling Chromatin Central in S. pombe. Table S6: physical properties and bioinformatic annotations of proteomics hyperlinks.
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Additional data file 2:
Figure S1: A-indices of six protein standards versus corresponding protein loadings. Figure S2: gel images of immunoprecipitation experiments used for compiling Chromatin Central in S. cerevisiae. Figure S3: multiple sequence alignments for several members of Chromatin Central in S. cerevisiae, whose similarity to corresponding S. pombe proteins was marginal. Figure S4: mass spectrometric identification of the novel 17 kDa protein in S. pombe, its full-length amino acid sequence and its alignment with the corresponding region of the genome. Figure S5: a plausible molecular architecture of the human Chromatin Central (partly supported by already published evidence). Table S5: domain composition of orthologous complexes within Chromatin Central in both yeasts. Table S7: plausible members of human Chromatin Central, considering their homology to corresponding proteins in both yeast proteomic environments and other published evidences.
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