Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1391647 | Chemistry & Biology | 2008 | 10 Pages |
SummaryAklanonic acid is synthesized by a type II polyketide synthase (PKS) composed of eight protein subunits. The network of protein interactions within this complex was investigated using a yeast two-hybrid system, by coaffinity chromatography and by two different computer-aided protein docking simulations. Results suggest that the ketosynthase (KS) α and β subunits interact with each other, and that the KSα subunit also probably interacts with a malonyl-CoA:ACP acyltransferase (DpsD), forming a putative minimal synthase. We speculate that DpsD may physically inhibit the priming reaction, allowing the choice of propionate rather than acetate as the starter unit. We also suggest a structural role for the cyclase (DpsY) in maintaining the overall structural integrity of the complex.