Complexome of Escherichia coli cytosolic proteins under normal native conditions
Date
2011-01-30Author
Pan, Jian-Yi (Zhejiang Sci-Tech University)
Wu, Hongkai (Sun Yat Sen Univ)
Liu, Xiang (Sun Yat Sen Univ)
Li, Pei-Pei (Sun Yat Sen Univ)
Li, Hui (Sun Yat Sen Univ)
Wang, San-Ying
王三英
Peng, Xuan-Xian (Sun Yat Sen Univ)
Collections
- 生命科学-已发表论文 [5876]
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. 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.
Citation
Mol. BioSyst., 2011, 7, 2651-2663URI
http://dx.doi.org/doi:10.1039/C1MB05103BWOS:000293648300014
https://dspace.xmu.edu.cn/handle/2288/12071