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首页> 外文期刊>Applied Microbiology >The Phospholipid:Diacylglycerol Acyltransferase-Mediated Acyl-Coenzyme A-Independent Pathway Efficiently Diverts Fatty Acid Flux from Phospholipid into Triacylglycerol in Escherichia coli
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The Phospholipid:Diacylglycerol Acyltransferase-Mediated Acyl-Coenzyme A-Independent Pathway Efficiently Diverts Fatty Acid Flux from Phospholipid into Triacylglycerol in Escherichia coli

机译：磷脂：二酰基甘油酰基转移酶介导的酰基 - 辅酶A-无关的途径有效地将脂肪酸通量从磷脂中转移到大肠杆菌中的三酰基甘油中

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Researchers have long endeavored to accumulate triacylglycerols (TAGs) or their derivatives in easily managed microbes. The attempted production of TAGs in Escherichia coli has revealed barriers to the broad applications of this technology, including low TAG productivity and slow cell growth. We have demonstrated that an acyl-CoA-independent pathway can divert phospholipid flux into TAG formation in E. coli mediated by Chlamydomonas reinhardtii phospholipid:diacylglycerol acyltransferase (CrPDAT) without interfering with membrane functions. We then showed the synergistic effect on TAG accumulation via the acyl-CoA-independent pathway mediated by PDAT and the acyl-CoA-dependent pathway mediated by wax ester synthase/acyl-CoA:diacylglycerol acyltransferase (WS/DGAT). Furthermore, CrPDAT led to synchronous TAG accumulation during cell growth, and this could be enhanced by supplementation of arbutin. We also showed that rationally mutated CrPDAT was capable of decreasing TAG lipase activity without impairing PDAT activity. Finally, ScPDAT from Saccharomyces cerevisiae exhibited similar activities as CrPDAT in E. coli . Our results suggest that the improvement in accumulation of TAGs and their derivatives can be achieved by fine-tuning of phospholipid metabolism in E. coli . Understanding the roles of PDAT in the conversion of phospholipids into TAGs during the logarithmic growth phase may enable a novel strategy for the production of microbial oils.IMPORTANCE Although phospholipid:diacylglycerol acyltransferase (PDAT) activity is presumed to exist in prokaryotic oleaginous bacteria, the corresponding gene has not been identified yet. In this article, we have demonstrated that an acyl-CoA-independent pathway can divert phospholipid flux into TAG formation in Escherichia coli mediated by exogenous CrPDAT from Chlamydomonas reinhardtii without interfering with membrane functions. In addition, the acyl-CoA-independent pathway and the acyl-CoA-dependent pathway had the synergistic effect on TAG accumulation. Overexpression of CrPDAT led to synchronous TAG accumulation during cell growth. In particular, CrPDAT possessed multiple catalytic activities, and the rational mutation of CrPDAT led to the decrease of TAG lipase activity without impairing acyltransferase activity. The present findings suggested that applying PDAT in E. coli or other prokaryotic microbes may be a promising strategy for accumulation of TAGs and their derivatives.
机译：研究人员长期努力在易于管理微生物中积累三酰基甘油（标签）或其衍生物。 Escherichia Coli中的标签的尝试生产揭示了这项技术广泛应用的障碍，包括低标签生产率和缓慢的细胞生长。我们已经证明了酰基 - CoA无关的途径可以将磷脂通量转移到由Chlamydomonas Reinhardtii磷脂介导的大肠杆菌中的标签形成中：二酰基甘油酰基转移酶（CRPDAT）而不干扰膜功能。然后，我们通过PDAT介导的酰基-CoA - 依赖于酰基-COA依赖性途径和由蜡酯合酶/酰基-COA介导的酰基-COA依赖性途径：二酰基甘油酰基转移酶（WS / DGAT）介导的酰基-COA依赖性途径的协同作用。此外，CRPDAT导致细胞生长期间的同步标签积累，并且可以通过补充arbutin来提高这一点。我们还表明，理性突变的CRPDAT能够降低标签脂肪酶活性而不损害PDAT活性。最后，Saccharomyces Cerevisiae的SCPDAT在大肠杆菌中表现出与CRPDAT类似的活动。我们的研究结果表明，通过在大肠杆菌中的磷脂代谢微调来实现标签和其衍生物积累的改善。理解PDAT在对数生长阶段转换为标签中的PDAT的作用，可以使微生物油的产生新的策略。虽然磷脂：磷脂：二氨基甘油酰基转移酶（PDAT）活性被假定在原核植物细菌中存在，相应的尚未确定基因。在本文中，我们已经证明了酰基 - CoA独立的途径可以将磷脂通量转移到由衣原体Reinhardtii的外源CRPDAT介导的大肠杆菌中的标签形成中，而不会干扰膜功能。另外，酰基 - 辅酶依赖性途径和酰基-CoA依赖性途径对标签积累具有协同作用。 CRPDAT的过度表达导致细胞生长过程中的同步标签积累。特别地，CRPDAT具有多种催化活性，CRPDAT的合理突变导致标签脂肪酶活性的降低而不损害酰基转移酶活性。本研究结果表明，在大肠杆菌或其他原核微生物中施加PDAT可能是积累标签及其衍生物的有希望的策略。

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