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The biosynthetic pathways for the fungal polyketides bikaverin and bostrycoidin, from  Fusarium verticillioides  and  Fusarium solani  respectively, were reconstructed and heterologously expressed in  S. cerevisiae  alongside seven different phosphopantetheinyl transferases (PPTases) from a variety of origins spanning bacterial, yeast and fungal origins. In order to gauge the efficiency of the interaction between the ACP-domains of the polyketide synthases (PKS) and PPTases, each were co-expressed individually and the resulting production of target polyketides were determined after 48 h of growth. In co-expression with both biosynthetic pathways, the PPTase from  Fusarium verticillioides  (FvPPT1) proved most efficient at producing both bikaverin and bostrycoidin, at 1.4 mg/L and 5.9 mg/L respectively. Furthermore, the remaining PPTases showed the ability to interact with both PKS’s, except for a single PKS-PPTase combination. The results indicate that it is possible to boost the production of a target polyketide, simply by utilizing a more optimal PPTase partner, instead of the commonly used PPTases; NpgA, Gsp and Sfp, from  Aspergillus nidulans ,  Brevibacillus brevis  and  Bacillus subtilis  respectively.

Speed dating for enzymes! Finding the perfect phosphopantetheinyl transferase partner for your polyketide synthase