Jump to main content
Jump to site search

Issue 9, 2011
Previous Article Next Article

Complexome of Escherichia coli cytosolic proteins under normal native conditions

Author affiliations

Abstract

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. coliK-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.

Graphical abstract: Complexome of Escherichia coli cytosolic proteins under normal native conditions

Back to tab navigation

Supplementary files

Publication details

The article was received on 13 Mar 2011, accepted on 17 May 2011 and first published on 30 Jun 2011


Article type: Paper
DOI: 10.1039/C1MB05103B
Mol. BioSyst., 2011,7, 2651-2663

  •   Request permissions

    Complexome of Escherichia coli cytosolic proteins under normal native conditions

    J. Pan, H. Wu, X. Liu, P. Li, H. Li, S. Wang and X. Peng, Mol. BioSyst., 2011, 7, 2651
    DOI: 10.1039/C1MB05103B

Search articles by author

Spotlight

Advertisements