Relationship between semantic distance and the proportion of pairs within each duplicate set

<p><b>Copyright information:</b></p><p>Taken from "All duplicates are not equal: the difference between small-scale and genome duplication"</p><p>http://genomebiology.com/2007/8/10/R209</p><p>Genome Biology 2007;8(10):R209-R209.</p><p>Published online 4 Oct 2007</p><p>PMCID:PMC2246283.</p><p></p> Whole-genome duplicates (WGDs) are illustrated in blue, small-scale duplicates (SSDs) in red, and random gene pairings in gray. A higher semantic distance indicates greater functional divergence

Relationship between semantic distance, duplicate set and complex membership

<p><b>Copyright information:</b></p><p>Taken from "All duplicates are not equal: the difference between small-scale and genome duplication"</p><p>http://genomebiology.com/2007/8/10/R209</p><p>Genome Biology 2007;8(10):R209-R209.</p><p>Published online 4 Oct 2007</p><p>PMCID:PMC2246283.</p><p></p> The proportion of duplicate pairs having a certain level of functional divergence as measured by semantic distance for the following: pairs of complex-forming whole-genome duplicate (WGD; dark blue), complex-forming small-scale duplicate (SSD; red), non-complex-forming WGD (light blue), and non-complex-forming SSD (pink) proteins. Significant differences in the degree of functional divergence between the pairs in the two categories (complex and non-complex) are observed. No significant difference between the semantic distances of pairs of SSDs found in complexes and complex-forming WGD pairs is observed; nor, indeed, is there any difference between SSD pairs not in complexes and WGD pairs not found within complexes

Visualization of the two sets of duplicates on a semantic distance network

<p><b>Copyright information:</b></p><p>Taken from "All duplicates are not equal: the difference between small-scale and genome duplication"</p><p>http://genomebiology.com/2007/8/10/R209</p><p>Genome Biology 2007;8(10):R209-R209.</p><p>Published online 4 Oct 2007</p><p>PMCID:PMC2246283.</p><p></p> The yeast proteome is distributed spatially according to semantic distance, with six high-level functional classes highlighted in different colors that are either over-represented or under-represented in the whole-genome duplicate (WGD) or small-scale duplicate (SSD) sets (see Table 1). WGDs are shown in blue and SSDs in red; the same six functional classes are highlighted. The products of the two types of duplicate gene have a tendency to occupy separate areas of semantic space, indicating involvement in different functions

Integration of proteome and metabolic control to show regulation of sulfur and C1 (folate) metabolic fluxes at the protein (enzyme) level

Selected proteins with levels consistently upregulated (red) or downregulated (green) with growth independently of culture conditions are shown. Sulfur, C1 metabolism, methyl cycle, methionine and -adenosylmethionine (SAM) fluxes towards methylation of proteins, rRNAs and tRNAs, and protein biosynthesis are shown here. Metabolic pathways and enzymes are from [42,82, 103-105] and the diagram is drawn with Cell Designer [136] and Adobe Illustrator [137]. Reverse methionine biosynthetic pathways [83] have been omitted for clarity. Metabolite abbreviations: THF, tetrahydrofolate; METTHF, 5,10-methylenetetrahydrofolate; MTHPTGLUT, 5-methyltetrahydropteroyltriglutamate (donor of the terminal methyl group in methionine biosynthesis); GT, glutathione; CYS, cysteine; CT, cystathionine; OAHS, -acetylhomoserine; HCYS, homocysteine; MET, methionine; SAM, -adenosylmethionine; SAH, -adenosylhomocysteine; D-SAM, decarboxylated -adenosylmethionine; MTA, methylthioadenosine. Metabolic steps (genes/enzymes): Met10p, sulfite reductase alpha subunit; Ecm17p, sulfite reductase beta subunit; , folylpolyglutamate synthetase (Met7p not detected; the relevance of polyglutamylation in the C1 metabolism branch was demonstrated at the transcriptional level (see text)); Met13p, methylenetetrahydrofolate reductase isozyme; Met6p, methionine synthase; Mes1p, methionyl-tRNA synthetase; Sam1p, S-adenosylmethionine synthetase isozyme; Sam2p, S-adenosylmethionine synthetase isozyme. Sah1p, S-adenosyl-L-homocysteine hydrolase; Ado1p, adenosine kinase.<p><b>Copyright information:</b></p><p>Taken from "Growth control of the eukaryote cell: a systems biology study in yeast"</p><p>http://jbiol.com/content/6/2/4</p><p>Journal of Biology 2007;6(2):4-4.</p><p>Published online 30 Apr 2007</p><p>PMCID:PMC2373899.</p><p></p

Integration of proteome and metabolic control to show regulation of carbon and nitrogen metabolic fluxes at the protein (enzyme) level

Shown here are the coupling of carbon and nitrogen fluxes at the level of glutamate dehydrogenase (Gdh1p, Gdh2p) and glutamine synthetase (Gln1p), the regulation of arginine biosynthesis at the carbamoyl phosphate synthetase (Cpa1p, Cpa2p) level and amino-acid biosynthesis, and amino-acid sensing by TOR. Selected proteins with levels consistently upregulated (red) with growth independently of culture conditions are shown. Enzymes responsible for the cytosolic 2-oxoglutarate pool: Aco1p and Aco2p, aconitase and putative aconitase isoenzyme; Odc1p and Odc2p, mitochondrial 2-oxoglutarate transporters; Idp2p, NADP-specific isocitrate dehydrogenase. Enzyme subunits coupling the oxidation of succinate to the transfer of electrons to ubiquinone: Sdh1p and Sdh2p, succinate dehydrogenase, flavoprotein, and iron-sulfur protein subunits, respectively. Metabolic diagram from [42, 91, 92] and drawn using Cell Designer [136] and Adobe Illustrator [137].<p><b>Copyright information:</b></p><p>Taken from "Growth control of the eukaryote cell: a systems biology study in yeast"</p><p>http://jbiol.com/content/6/2/4</p><p>Journal of Biology 2007;6(2):4-4.</p><p>Published online 30 Apr 2007</p><p>PMCID:PMC2373899.</p><p></p