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Toward production of jet fuel functionality in oilseeds: identification of FatB acyl-acyl carrier protein thioesterases and evaluation of combinatorial expression strategies in Camelina seeds.

Kim HJ, Silva JE, Vu HS, Mockaitis K, Nam JW, Cahoon EB - J. Exp. Bot. (2015)

Bottom Line: Expression of CpuFatB3 and CvFatB1 resulted in Camelina oil with capric acid (10:0), and CpuFatB4 expression conferred myristic acid (14:0) production and increased 16:0.Increases in lauric acid (12:0) and 14:0, but not 10:0, in Camelina oil and at the sn-2 position of triacylglycerols resulted from inclusion of a coconut lysophosphatidic acid acyltransferase specialized for MCFAs.Camelina lines presented here provide platforms for additional metabolic engineering targeting fatty acid synthase and specialized acyltransferases for achieving oils with high levels of jet fuel-type fatty acids.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry and Center for Plant Science Innovation, University of Nebraska-Lincoln, Lincoln, NE 68588, USA.

No MeSH data available.


Related in: MedlinePlus

Acyl-ACP analysis of developing seeds of Cuphea viscosissima and wild-type and transgenic Camelina seeds. Shown in (A) are acyl-ACP pools in developing seeds of C. viscosissima. Shown in (B) are acyl-ACP profiles in wild-type Camelina (WT) and transgenic Camelina seeds expressing UcFATB1, CpuFATB1, and ChFatB2 at 15 DAF. The data are means ±SD of five biological replicates.
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Figure 8: Acyl-ACP analysis of developing seeds of Cuphea viscosissima and wild-type and transgenic Camelina seeds. Shown in (A) are acyl-ACP pools in developing seeds of C. viscosissima. Shown in (B) are acyl-ACP profiles in wild-type Camelina (WT) and transgenic Camelina seeds expressing UcFATB1, CpuFATB1, and ChFatB2 at 15 DAF. The data are means ±SD of five biological replicates.

Mentions: The expression of FatB genes from Cuphea results in increased MCFA levels in Camelina seed oils, but does not approach the levels of MCFA that occur naturally in Cuphea seeds. This may be due to the evolution of substrate specificity within the components of the FAS complex in Cuphea species. To examine this hypothesis, the acyl-ACP composition of developing seeds from C. viscosissima and Camelina was analysed by electrospray ionization-tandem mass spectrometry (ESI-MS/MS) (Fig. 8). Acyl-ACP pool sizes were estimated based on comparison of relative peak area percentages per unit of protein analysed. In C. viscosissima, 8:0-ACP made up 40% of the acyl-ACP pools, followed by 10:0-ACP (24%) and 6:0-ACP (19%). Long-chain (≥16) acyl-ACPs were barely detected and made up <1% of total acyl-ACP in developing seeds of C. viscosissima. In contrast, acyl-ACP pools of transgenic and wild-type Camelina seeds were increased at 10 days after flowering (DAF) (Supplementary Fig. S4 at JXB online). However, increased percentages of 8:0, 10:0, and 12:0 ACPs were detected in 15 DAF developing seeds from FatB transgenic lines compared with wild-type seeds.


Toward production of jet fuel functionality in oilseeds: identification of FatB acyl-acyl carrier protein thioesterases and evaluation of combinatorial expression strategies in Camelina seeds.

Kim HJ, Silva JE, Vu HS, Mockaitis K, Nam JW, Cahoon EB - J. Exp. Bot. (2015)

Acyl-ACP analysis of developing seeds of Cuphea viscosissima and wild-type and transgenic Camelina seeds. Shown in (A) are acyl-ACP pools in developing seeds of C. viscosissima. Shown in (B) are acyl-ACP profiles in wild-type Camelina (WT) and transgenic Camelina seeds expressing UcFATB1, CpuFATB1, and ChFatB2 at 15 DAF. The data are means ±SD of five biological replicates.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4493788&req=5

Figure 8: Acyl-ACP analysis of developing seeds of Cuphea viscosissima and wild-type and transgenic Camelina seeds. Shown in (A) are acyl-ACP pools in developing seeds of C. viscosissima. Shown in (B) are acyl-ACP profiles in wild-type Camelina (WT) and transgenic Camelina seeds expressing UcFATB1, CpuFATB1, and ChFatB2 at 15 DAF. The data are means ±SD of five biological replicates.
Mentions: The expression of FatB genes from Cuphea results in increased MCFA levels in Camelina seed oils, but does not approach the levels of MCFA that occur naturally in Cuphea seeds. This may be due to the evolution of substrate specificity within the components of the FAS complex in Cuphea species. To examine this hypothesis, the acyl-ACP composition of developing seeds from C. viscosissima and Camelina was analysed by electrospray ionization-tandem mass spectrometry (ESI-MS/MS) (Fig. 8). Acyl-ACP pool sizes were estimated based on comparison of relative peak area percentages per unit of protein analysed. In C. viscosissima, 8:0-ACP made up 40% of the acyl-ACP pools, followed by 10:0-ACP (24%) and 6:0-ACP (19%). Long-chain (≥16) acyl-ACPs were barely detected and made up <1% of total acyl-ACP in developing seeds of C. viscosissima. In contrast, acyl-ACP pools of transgenic and wild-type Camelina seeds were increased at 10 days after flowering (DAF) (Supplementary Fig. S4 at JXB online). However, increased percentages of 8:0, 10:0, and 12:0 ACPs were detected in 15 DAF developing seeds from FatB transgenic lines compared with wild-type seeds.

Bottom Line: Expression of CpuFatB3 and CvFatB1 resulted in Camelina oil with capric acid (10:0), and CpuFatB4 expression conferred myristic acid (14:0) production and increased 16:0.Increases in lauric acid (12:0) and 14:0, but not 10:0, in Camelina oil and at the sn-2 position of triacylglycerols resulted from inclusion of a coconut lysophosphatidic acid acyltransferase specialized for MCFAs.Camelina lines presented here provide platforms for additional metabolic engineering targeting fatty acid synthase and specialized acyltransferases for achieving oils with high levels of jet fuel-type fatty acids.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry and Center for Plant Science Innovation, University of Nebraska-Lincoln, Lincoln, NE 68588, USA.

No MeSH data available.


Related in: MedlinePlus