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Updated: Jul 8, 2026
13:51
The MultiBac Protein Complex Production Platform at the EMBL
Published on: July 11, 2013
Interaction network containing conserved and essential protein complexes in Escherichia coli
Gareth Butland1, José Manuel Peregrín-Alvarez, Joyce Li
1Banting and Best Department of Medical Research, University of Toronto, 112 College Street, Toronto, Ontario M5G 1L6, Canada.
Nature
|February 4, 2005
Summary
This study mapped protein complexes in Escherichia coli, revealing a network of interactions for over 600 proteins. This provides new insights into bacterial protein functions and conserved microbial networks.
Area of Science:
- Microbiology
- Proteomics
- Systems Biology
Background:
- Proteins function in multi-subunit complexes, crucial for cellular processes.
- Escherichia coli is a long-standing model organism, yet large-scale protein complex analysis was lacking.
Purpose of the Study:
- To conduct a large-scale analysis of protein complexes in Escherichia coli.
- To uncover and validate an interaction network of these complexes.
Main Methods:
- Targeted DNA cassettes to create affinity-tagged alleles for 1,000 open reading frames in E. coli.
- Purification of 648 proteins to homogeneity.
- Identification of interacting protein partners using mass spectrometry.
Main Results:
- Successfully tagged 857 proteins, including conserved essential proteins.
- Identified protein interaction partners for 648 purified proteins.
- Uncovered and validated an interaction network of protein complexes involved in diverse biological processes.
Conclusions:
- The study provides insights into the function of uncharacterized bacterial proteins.
- Reveals the topology of a microbial interaction network with broadly conserved core components across Prokaryota.
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