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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

Alignment of deduced Cuphea FatB acyl-ACP thioesterases. Identical amino acids are shaded in black; conserved residues are shaded in grey. The triangle indicates the predicted site of the transit peptide.
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Figure 4: Alignment of deduced Cuphea FatB acyl-ACP thioesterases. Identical amino acids are shaded in black; conserved residues are shaded in grey. The triangle indicates the predicted site of the transit peptide.

Mentions: Based on sequence homology and substrate chain length specificities, Cuphea FatB proteins have been classified into three groups: clade I generally has preferential activity towards 16:0-ACP; clade II generally has preferential activity towards 12:0-ACP and 14:0-ACP or broad-range specificity (12:0-ACP to 16:0-ACP); and clade III generally has preferential activity towards 8:0-ACP and 10:0-ACP (Voelker, 1996; Filichkin et al., 2006; Jing et al., 2011). Alignment of deduced FatBs from six Cuphea species showed that C. pulcherrima and C. viscosissima FatB genes could be grouped as seed-specific CpuFatB3 and CvFatB1 (clade III), CpuFatB4 and CvFatB3 (Clade II), and CpuFatB1, CpuFatB2, and CvFatB2 (clade I) (Fig. 3). The identity of amino acid sequences among Cuphea FatB polypeptides ranged from 70% to 93%. The chloroplast transit peptides were predicted based on homology with known FatBs (Fig. 4).


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)

Alignment of deduced Cuphea FatB acyl-ACP thioesterases. Identical amino acids are shaded in black; conserved residues are shaded in grey. The triangle indicates the predicted site of the transit peptide.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

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

Figure 4: Alignment of deduced Cuphea FatB acyl-ACP thioesterases. Identical amino acids are shaded in black; conserved residues are shaded in grey. The triangle indicates the predicted site of the transit peptide.
Mentions: Based on sequence homology and substrate chain length specificities, Cuphea FatB proteins have been classified into three groups: clade I generally has preferential activity towards 16:0-ACP; clade II generally has preferential activity towards 12:0-ACP and 14:0-ACP or broad-range specificity (12:0-ACP to 16:0-ACP); and clade III generally has preferential activity towards 8:0-ACP and 10:0-ACP (Voelker, 1996; Filichkin et al., 2006; Jing et al., 2011). Alignment of deduced FatBs from six Cuphea species showed that C. pulcherrima and C. viscosissima FatB genes could be grouped as seed-specific CpuFatB3 and CvFatB1 (clade III), CpuFatB4 and CvFatB3 (Clade II), and CpuFatB1, CpuFatB2, and CvFatB2 (clade I) (Fig. 3). The identity of amino acid sequences among Cuphea FatB polypeptides ranged from 70% to 93%. The chloroplast transit peptides were predicted based on homology with known FatBs (Fig. 4).

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