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Background  Phosphatidic acid phosphatase (PAP, EC 3.1.3.4) catalyzes the dephosphorylation of phosphatidate yielding diacylglycerol (DAG), the lipid precursor for triacylglycerol (TAG) biosynthesis. Despite the importance of PAP activity in TAG producing bacteria, studies to establish its role in lipid metabolism have been so far restricted only to eukaryotes. Considering the increasing interest of bacterial TAG as a potential source of raw material for biofuel production, we have focused our studies on the identification and physiological characterization of the putative PAP present in the TAG producing bacterium  Streptomyces coelicolor .    Results  We have identified two  S. coelicolor  genes, named  lppα  (SCO1102) and  lppβ  (SCO1753), encoding for functional PAP proteins. Both enzymes mediate, at least in part, the formation of DAG for neutral lipid biosynthesis. Heterologous expression of  lppα  and  lppβ  genes in  E. coli  resulted in enhanced PAP activity in the membrane fractions of the recombinant strains and concomitantly in higher levels of DAG. In addition, the expression of these genes in yeast complemented the temperature-sensitive growth phenotype of the PAP deficient strain GHY58 ( dpp1lpp1pah1 ). In  S. coelicolor , disruption of either  lppα  or  lppβ  had no effect on TAG accumulation; however, the simultaneous mutation of both genes provoked a drastic reduction in  de novo  TAG biosynthesis as well as in total TAG content. Consistently, overexpression of Lppα and Lppβ in the wild type strain of  S. coelicolor  led to a significant increase in TAG production.    Conclusions  The present study describes the identification of PAP enzymes in bacteria and provides further insights on the genetic basis for prokaryotic oiliness. Furthermore, this finding completes the whole set of enzymes required for  de novo  TAG biosynthesis pathway in  S. coelicolor . Remarkably, the overexpression of these PAPs in  Streptomyces  bacteria contributes to a higher productivity of this single cell oil. Altogether, these results provide new elements and tools for future cell engineering for next-generation biofuels production.

microbial cell factories

Identification and physiological characterization of phosphatidic acid phosphatase enzymes involved in triacylglycerol biosynthesis in Streptomyces coelicolor