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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.

SUBMITTER: Rothmann M

PROVIDER: S-EPMC3809020 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature

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

Rothmann Michael M Niessen Sherry S Haushalter Robert W RW Cravatt Benjamin F BF Burkart Michael D MD

Bioorganic & medicinal chemistry 20111031 2

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 bi ...[more]

PMID: 22104437

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