Journal Article

DKFZ-2018-00256

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The binary protein-protein interaction landscape of Escherichia coli.

Rajagopala, S. V. ; Sikorski, P. ; Kumar, A. ; Mosca, R. ; Vlasblom, J. ; Arnold, R. ; Franca-Koh, J. ; Pakala, S. B. ; Phanse, S. ; Ceol, A. ; Häuser, R.DKFZ* ; Siszler, G.DKFZ* ; Wuchty, S. ; Emili, A. ; Babu, M. ; Aloy, P. ; Pieper, R. ; Uetz, P.

2014
Nature America New York, NY

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Please use a persistent id in citations: doi:10.1038/nbt.2831

Abstract: Efforts to map the Escherichia coli interactome have identified several hundred macromolecular complexes, but direct binary protein-protein interactions (PPIs) have not been surveyed on a large scale. Here we performed yeast two-hybrid screens of 3,305 baits against 3,606 preys (∼70% of the E. coli proteome) in duplicate to generate a map of 2,234 interactions, which approximately doubles the number of known binary PPIs in E. coli. Integration of binary PPI and genetic-interaction data revealed functional dependencies among components involved in cellular processes, including envelope integrity, flagellum assembly and protein quality control. Many of the binary interactions that we could map in multiprotein complexes were informative regarding internal topology of complexes and indicated that interactions in complexes are substantially more conserved than those interactions connecting different complexes. This resource will be useful for inferring bacterial gene function and provides a draft reference of the basic physical wiring network of this evolutionarily important model microbe.

Keyword(s): Escherichia coli Proteins

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Contributing Institute(s):

1. Proteininteraktion (W150)

Research Program(s):

1. 312 - Functional and structural genomics (POF3-312) (POF3-312)

Appears in the scientific report 2014

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