title: Resin-based investigation of acyl carrier protein interaction networks in Escherichia coli.
abstract: Protein-protein interactions play an integral role in metabolic regulation. Elucidation of these networks is complicated by the changing identity of the proteins themselves. Here we demonstrate a resin-based technique that leverages the unique tools for acyl carrier protein (ACP) modification with non-hydrolyzable linkages. ACPs from Escherichia coli and Shewanella oneidensis MR-1 are bound to Affigel-15 with varying acyl groups attached and introduced to proteomic samples. Isolation of these binding partners is followed by MudPIT analysis to identify each interactome with the variable of ACP-tethered substrates. These techniques allow for investigation of protein interaction networks with the changing identity of a given protein target.
authors: Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0358, USA.
authors: Michael
authors: M
authors: Rothmann
authors: Sherry
authors: S
authors: Niessen
authors: Robert W
authors: RW
authors: Haushalter
authors: Benjamin F
authors: BF
authors: Cravatt
authors: Michael D
authors: MD
authors: Burkart
mesh_terms: D000213:Acyl Carrier Protein / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D013058:Mass Spectrometry; D010204:Pantetheine / Q000737:chemistry; D025941:Protein Interaction Mapping; D012117:Resins, Synthetic / Q000737:chemistry*; D020592:Shewanella / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D000213:Acyl Carrier Protein; D012117:Resins, Synthetic; D010204:Pantetheine