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Elucidating the dynamic remodelling of Escherichia Coli interactome in different growth conditions using multiplex co-fractionation MS (mCF-MS)
  • Teck Yew Low
Teck Yew Low
UKM Medical Molecular Biology Institute (UMBI)

Corresponding Author:[email protected]

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Most proteins function by forming complexes within a dynamic interconnected network that underlies various biological mechanisms. To systematically investigate such interactomes, high-throughput techniques including CF-MS have been developed to capture, identify, and quantify protein-protein interactions (PPIs) in large-scale. Compared to other techniques, CF-MS allows the global identification and quantification of native protein complexes in one setting, without genetic manipulation and overexpression. Furthermore, quantitative CF-MS can potentially elucidate the distribution of a protein in multiple co-elution features, informing the stoichiometries and dynamics of a target protein complex. In this issue, Youssef et al. (Proteomics 2023, XX, XXXX-XXXX) combined multiplex CF-MS and an in-house algorithm to study the dynamics of the PPI network for Escherichia coli grown under ten different conditions. While the results demonstrated that while most proteins remained stable, the authors were able to detect disrupted interactions that were growth condition-specific. Further bioinformatics analyses also revealed biophysical properties and structural patterns that govern such a response.
23 May 2023Submitted to PROTEOMICS
23 May 2023Assigned to Editor
23 May 2023Submission Checks Completed
23 May 2023Review(s) Completed, Editorial Evaluation Pending
25 May 2023Editorial Decision: Revise Minor
27 May 2023Review(s) Completed, Editorial Evaluation Pending
27 May 20231st Revision Received
05 Jun 2023Editorial Decision: Accept