Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, Corrensstrasse 3, Münster, Germany.
Appl Environ Microbiol. 2010 May;76(9):2884-94. doi: 10.1128/AEM.02832-09. Epub 2010 Mar 19.
In many microorganisms, the key enzyme responsible for catalyzing the last step in triacylglycerol (TAG) and wax ester (WE) biosynthesis is an unspecific acyltransferase which is also referred to as wax ester synthase/acyl coenzyme A (acyl-CoA):diacylglycerol acyltransferase (WS/DGAT; AtfA). The importance and function of two AtfA homologues (AtfA1 and AtfA2) in the biosynthesis of TAGs and WEs in the hydrocarbon-degrading marine bacterium Alcanivorax borkumensis SK2 have been described recently. However, after the disruption of both the AtfA1 and AtfA2 genes, reduced but substantial accumulation of TAGs was still observed, indicating the existence of an alternative TAG biosynthesis pathway. In this study, transposon-induced mutagenesis was applied to an atfA1 atfA2 double mutant to screen for A. borkumensis mutants totally defective in biosynthesis of neutral lipids in order to identify additional enzymes involved in the biosynthesis of these lipids. At the same time, we have searched for a totally TAG-negative mutant in order to study the function of TAGs in A. borkumensis. Thirteen fluorescence-negative mutants were identified on Nile red ONR7a agar plates and analyzed for their abilities to synthesize lipids. Among these, mutant 2 M(131) was no longer able to synthesize and accumulate TAGs if pyruvate was used as the sole carbon source. The transposon insertion was localized in a gene encoding a putative cytochrome c family protein (ABO_1185). Growth and TAG accumulation experiments showed that the disruption of this gene resulted in the absence of TAGs in 2 M(131) but that growth was not affected. In cells of A. borkumensis SK2 grown on pyruvate as the sole carbon source, TAGs represented about 11% of the dry weight of the cells, while in the mutant 2 M(131), TAGs were not detected by thin-layer and gas chromatography analyses. Starvation and lipid mobilization experiments revealed that the lipids play an important role in the survival of the cells. The function of neutral lipids in A. borkumensis SK2 is discussed.
在许多微生物中,负责催化甘油三酯 (TAG) 和蜡酯 (WE) 生物合成最后一步的关键酶是一种非特异性酰基转移酶,也称为蜡酯合酶/酰基辅酶 A(酰基-CoA):二酰基甘油酰基转移酶 (WS/DGAT; AtfA)。最近已经描述了两种 AtfA 同源物 (AtfA1 和 AtfA2) 在烃降解海洋细菌 Alcanivorax borkumensis SK2 中 TAG 和 WE 生物合成中的重要性和功能。然而,在敲除 AtfA1 和 AtfA2 基因后,仍观察到 TAG 的积累减少但仍相当可观,表明存在替代的 TAG 生物合成途径。在这项研究中,转座子诱导的诱变被应用于 atfA1 atfA2 双突变体,以筛选中性脂质生物合成完全缺陷的 A. borkumensis 突变体,以鉴定参与这些脂质生物合成的其他酶。同时,我们还寻找了一个完全不含 TAG 的突变体,以研究 TAG 在 A. borkumensis 中的功能。在 Nile red ONR7a 琼脂平板上鉴定出 13 个荧光阴性突变体,并分析它们合成脂质的能力。其中,突变体 2 M(131)如果使用丙酮酸作为唯一碳源,则不再能够合成和积累 TAG。转座子插入定位于编码假定细胞色素 c 家族蛋白 (ABO_1185) 的基因中。生长和 TAG 积累实验表明,该基因的破坏导致 2 M(131)中没有 TAG,但生长不受影响。在以丙酮酸为唯一碳源生长的 A. borkumensis SK2 细胞中,TAG 约占细胞干重的 11%,而在突变体 2 M(131)中,通过薄层层析和气相色谱分析未检测到 TAGs。饥饿和脂质动员实验表明,脂质在细胞存活中起着重要作用。讨论了中性脂质在 A. borkumensis SK2 中的功能。