Protein-protein interactions play an integral role in metabolic regulation. We demonstrate a resin-based technique that leverages unique tools for acyl carrier protein (ACP) modification with non-hydrolyzable linkages. ACPs from Ecscherichia coli and Shewanella oneidensis MR-1 are bound to Affigel-15 with varying acyl groups attached and introduced to proteomic samples. Isolation of binding partners is followed by MudPIT analysis to identify each interactome. These techniques allow for investigation of protein interaction networks with the changing identity of a given protein target. 

Resin-based investigation of acyl carrier protein interaction networks in Escherichia coli

243rd National Meeting (2012)

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