Journal
MOLECULAR BIOSYSTEMS
Volume 7, Issue 9, Pages 2651-2663Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c1mb05103b
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Funding
- NSFC [30972279, 40976080]
- Sun Yat-sen University [10lgzd03, SKLBC09B04]
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The 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.
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