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Abstract:
Pairs of docking domains (DDs) mediate the selective interations between adjacent nonribosomal peptide synthetases (NRPSs) to form defined protein-protein interactions resulting in defined peptide sequences. New specific rhabdopeptide/xenortide-like peptides (RXPs) were generated by swapping of either flexible or nonfunctional DD pairs between these monomodular RXP-NRPSs against DDs from collinear NRPSs. The results presented a promising means of engineering RXP-producing NRPSs to obtain desired peptides and further substantiated the decisive role of DDs in the NRP synthesis.
