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dc.contributor.authorPan, Jian-Yi (Zhejiang Sci-Tech University)
dc.contributor.authorWu, Hongkai (Sun Yat Sen Univ)
dc.contributor.authorLiu, Xiang (Sun Yat Sen Univ)
dc.contributor.authorLi, Pei-Pei (Sun Yat Sen Univ)
dc.contributor.authorLi, Hui (Sun Yat Sen Univ)
dc.contributor.authorWang, San-Ying
dc.contributor.author王三英
dc.contributor.authorPeng, Xuan-Xian (Sun Yat Sen Univ)
dc.date.accessioned2012-04-13T11:48:06Z
dc.date.available2012-04-13T11:48:06Z
dc.date.issued2011-01-30
dc.identifier.citationMol. BioSyst., 2011, 7, 2651-2663zh_CN
dc.identifier.issn1742-206X
dc.identifier.urihttp://dx.doi.org/doi:10.1039/C1MB05103B
dc.identifier.uriWOS:000293648300014
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/12071
dc.description.abstractThe interactions between proteins are important for the majority of biological functions and the interacting proteins are usually assembled into a complex. Knowing a set of protein complexes of a cell (complexome) is, therefore, essential for a better understanding and global view of cell functions. To visualize and identify the protein complexome of E. coli K-12 under normal native conditions on a proteome-wide scale, we developed an integrated proteomic platform with the combination of 2-D native/SDS-PAGE-based proteomics with co-immunoprecipitation, far-Western blotting, His-tag affinity purification and functional analysis, and used it to investigate the E. coli cytosolic complexome. A total of 24 distinct heteromeric and 8 homomeric protein complexes were identified. These complexes mainly contributed to glycolysis/gluconeogenesis, bioinformation processing, and cellular processes. Of the 24 hetereomeric complexes, 16 were reported for the first time, and 2 known complexes contained novel components that have not been reported previously based on DIP database search. Among them, RpoC-RpsA-Tig-GroL was found to be involved in transcriptional and co-translational folding, and EF-G-TufA-Tsf-RpsA linked a protein synthesis site with protein translational elongation factors. This systematic proteome analysis provides new insights into E. coli molecular systems biology.zh_CN
dc.description.sponsorshipNSFC[30972279, 40976080]; Sun Yat-sen University[10lgzd03, SKLBC09B04]zh_CN
dc.language.isoenzh_CN
dc.publisherROYAL SOC CHEMISTRYzh_CN
dc.titleComplexome of Escherichia coli cytosolic proteins under normal native conditionszh_CN
dc.typeArticlezh_CN


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