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E. coli network upgrade

Nature Biotechnology volume 32, pages 241–243 (2014)Cite this article

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Combining yeast two-hybrid data with mass-spectrometry and structural data provides a detailed view of the E. coli interactome.

Protein interaction networks are crucial for understanding complex cellular systems, from how signals are processed and lead to cellular phenotypes to the function of individual network components under specific conditions. High-quality, binary protein-protein interaction maps have been generated for human cells and for many model organisms, including yeast, worm, fly and Arabidopsis thaliana. Now, Escherichia coli has joined this group with a study by Rajagopala et al.1 in this issue. Using yeast two-hybrid analysis, the authors construct a binary interaction network for E. coli that contains 2,234 protein-protein interactions between 1,850 proteins. These data, which include both transient interactions and more stable interactions within protein complexes, are then integrated with previous data on protein complexes and protein structure to produce a high-resolution E. coli interactome map—the most detailed map of its kind for any organism.

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Figure 1: The path toward a detailed, high-resolution E. coli interactome map starts by combining binary protein-protein interaction data from yeast two-hybrid analysis and data from affinity purification–MS5,6,7.

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  1. Ulrich Stelzl is at the Max Planck Institute for Molecular Genetics (MPIMG), Berlin, Germany.

    Ulrich Stelzl

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  1. Ulrich Stelzl
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Correspondence to Ulrich Stelzl.

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Stelzl, U. E. coli network upgrade. Nat Biotechnol 32, 241–243 (2014). https://doi.org/10.1038/nbt.2848

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