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Proteins predicted to participate in multi-protein structures such as cell division and O-antigen biosynthesis, and prone to aggregation based on relative abundance in insoluble E. coli O157:H7 fraction.

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Figshare2015-12-02 更新2026-04-29 收录
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A: Hierarchical clustering analysis using the Euclidian distance metric in MeV featuring groups of proteins with similar abundance patterns in the three SEC fractions compared to insoluble E. coli strain 86-24 lysate fraction. Clusters are visualized in Figure S2 (Suppl. Information). C1, C2 and C3 clusters contained many proteins part of large subcellular assemblies; o.C: other cluster; n.d. not significant in W-test.B: Gene name, locus tag and protein description are derived from annotations in the E. coli O157:H7 EDL933 genome (UniProt database) or the EcoCyc database. The first 19 genes/proteins have been associated with biosynthesis of the ‘O157’ O-antigen of EHEC serotype O157:H7. The next 12 genes/proteins have been associated with the cytoskeleton and cell (or plasmid) division. The flippase Wzx and polymerase Wzy, also part of the O-antigen biosynthesis apparatus and rich in transmembrane domains were not observed.C: Subcellular localization of proteins derived from EcoCyc data or annotations in UniProt for the EDL933 genome. CY: cytoplasm; IM: inner membrane; Z-ring: Z-ring formation during cell division septation; pIM: peripheral IM protein.D: Average protein abundances (APEXi scores) in the combined size exclusion chromatography (SEC) fractions (F1–39) pertaining to the soluble lysate fraction and the insoluble lysate fraction F4-p (F40–52). n = 11; APEXi normalization factor: 2.5×106; ‘0’: no peptide spectra were detected for a given protein.E: W-test: the Wilcoxon Rank Sum test was applied to the entire EHEC proteome dataset of 2521 proteins to select proteins with statistically significant abundance differences comparing the combined SEC fractions (F1–39; >280 kDa, 280-80 kDa and 80-10 kDa) with the insoluble lysate fraction F4-p. The proteins with a p-value of
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2015-12-02
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