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 (â ̂1/470% 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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 285-290 |
| Number of pages | 6 |
| Journal | Nature Biotechnology |
| Volume | 32 |
| Issue number | 3 |
| DOIs | |
| State | Published - 2014 |
Fingerprint
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology
- Biotechnology
- Molecular Medicine
- Bioengineering
- Biomedical Engineering
- Medicine(all)
Cite this
The binary protein-protein interaction landscape of escherichia coli. / Rajagopala, Seesandra V.; Sikorski, Patricia; Kumar, Ashwani; Mosca, Roberto; Vlasblom, James; Arnold, Roland; Franca-Koh, Jonathan; Pakala, Suman B.; Phanse, Sadhna; Ceol, Arnaud; Häuser, Roman; Siszler, Gabriella; Wuchty, Stefan; Emili, Andrew; Babu, Mohan; Aloy, Patrick; Pieper, Rembert; Uetz, Peter.
In: Nature Biotechnology, Vol. 32, No. 3, 2014, p. 285-290.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The binary protein-protein interaction landscape of escherichia coli
AU - Rajagopala, Seesandra V.
AU - Sikorski, Patricia
AU - Kumar, Ashwani
AU - Mosca, Roberto
AU - Vlasblom, James
AU - Arnold, Roland
AU - Franca-Koh, Jonathan
AU - Pakala, Suman B.
AU - Phanse, Sadhna
AU - Ceol, Arnaud
AU - Häuser, Roman
AU - Siszler, Gabriella
AU - Wuchty, Stefan
AU - Emili, Andrew
AU - Babu, Mohan
AU - Aloy, Patrick
AU - Pieper, Rembert
AU - Uetz, Peter
PY - 2014
Y1 - 2014
N2 - 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 (â ̂1/470% 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.
AB - 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 (â ̂1/470% 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.
UR - http://www.scopus.com/inward/record.url?scp=84898648935&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84898648935&partnerID=8YFLogxK
U2 - 10.1038/nbt.2831
DO - 10.1038/nbt.2831
M3 - Article
C2 - 24561554
AN - SCOPUS:84898648935
VL - 32
SP - 285
EP - 290
JO - Nature Biotechnology
JF - Nature Biotechnology
SN - 1087-0156
IS - 3
ER -