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

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dc.citation.titleMicrobial Cell Factories
dc.citation.volume12
dc.creatorComba, Santiago
dc.creatorMenendez Bravo, Simón M.
dc.creatorArabolaza, Ana Lorena
dc.creatorGramajo, Hugo Cesar
dc.date.accessioned2024-07-25T17:19:39Z
dc.date.available2024-07-25T17:19:39Z
dc.date.issued2013-01-29
dc.description.abstractBackground: 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.
dc.description.filFil: Comba, Santiago. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina.
dc.description.filFil: Menendez Bravo, Simón M. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina.
dc.description.filFil: Arabolaza, Ana Lorena. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina.
dc.description.filFil: Gramajo, Hugo Cesar. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina.
dc.description.sponsorshipAgencia Nacional de Promoción Científica y Tecnológica (ANPCyT) PICT2008-1640, PICT 2011–2005
dc.format.extent1-12
dc.identifier.issn1475-2859
dc.identifier.urihttps://hdl.handle.net/2133/27472
dc.language.isoen
dc.publisherBMC
dc.relation.publisherversionhttps://microbialcellfactories.biomedcentral.com/articles/10.1186/1475-2859-12-9
dc.relation.publisherversionhttps://doi.org/10.1186/1475-2859-12-9
dc.rightsopenAccess
dc.rights.holderComba, Santiago
dc.rights.holderMenendez Bravo, Simón M.
dc.rights.holderArabolaza, Ana Lorena
dc.rights.holderGramajo, Hugo Cesar
dc.rights.holderUniversidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas
dc.rights.textAttribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectPAP
dc.subjectTriacylglycerol
dc.subjectOleaginous bacteria
dc.subjectLipid metabolism
dc.titleIdentification and physiological characterization of phosphatidic acid phosphatase enzymes involved in triacylglycerol biosynthesis in Streptomyces coelicolor
dc.typearticulo
dc.type.collectionarticulo
dc.type.versionpublishedVersion

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