Dataset Information

Dynamic Remodeling of Escherichia coli Interactome in Response to Environmental Perturbations

ABSTRACT: Here, we applied co-fractionation mass spectrometry and computational modeling to quantify and profile the interactions of ~2,000 proteins in the bacterium Escherichia coli cultured under ten distinct culture conditions. The resulting quantitative co-elution patterns revealed large-scale condition-dependent interaction remodeling among protein complexes involved in diverse biochemical pathways in response to the unique environmental challenges. Network-level analysis highlighted interactome-wide biophysical properties and structural patterns governing interaction remodeling. Our results provide evidence of the local and global plasticity of the E. coli interactome.

INSTRUMENT(S):

ORGANISM(S): Escherichia Coli

SUBMITTER: Carl White

LAB HEAD: Andrew Emili

PROVIDER: PXD041263 | Pride | 2025-11-27

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20190531_FB_Cofrac_Rep1_F1.mgf	Mgf
	20190531_FB_Cofrac_Rep1_F1.raw	Raw
	20190531_FB_Cofrac_Rep1_F10.mgf	Mgf
	20190531_FB_Cofrac_Rep1_F10.raw	Raw
	20190531_FB_Cofrac_Rep1_F11.mgf	Mgf

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Dynamic remodeling of Escherichia coli interactome in response to environmental perturbations.

Youssef Ahmed A Bian Fei F Paniikov Nicolai S NS Crovella Mark M Emili Andrew A

Proteomics 20230530 21-22

Proteins play an essential role in the vital biological processes governing cellular functions. Most proteins function as members of macromolecular machines, with the network of interacting proteins revealing the molecular mechanisms driving the formation of these complexes. Profiling the physiology-driven remodeling of these interactions within different contexts constitutes a crucial component to achieving a comprehensive systems-level understanding of interactome dynamics. Here, we apply co-f ...[more]

PMID: 37248827

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