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Type 1 diacylglycerol acyltransferases of Brassica napus preferentially incorporate oleic acid into triacylglycerol.

Aznar-Moreno J, Denolf P, Van Audenhove K, De Bodt S, Engelen S, Fahy D, Wallis JG, Browse J - J. Exp. Bot. (2015)

Bottom Line: Thorough understanding of the enzymology of oil accumulation is critical to the goal of modifying oilseeds for improved vegetable oil production.This strong sensitivity of the BnDGAT1 isozymes to the relative concentrations of acyl-CoA substrates substantially explains the observed fatty acid composition of B. napus seed oil.Understanding these enzymes that are critical for triacylglycerol synthesis will facilitate genetic and biotechnological manipulations to improve this oilseed crop.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340, USA.

No MeSH data available.


Related in: MedlinePlus

Separation of yeast lipids by TLC. Expression of each BnDGAT1 recovers TAG synthesis in yeast H1246, a TAG synthesis quadruple mutant (are1, are2, lro1, dga1). The mutant transformed with the empty vector served as negative control. The wild type is SCY62, and the right lane is the TAG standard. Triacylglycerols are boxed.
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Figure 4: Separation of yeast lipids by TLC. Expression of each BnDGAT1 recovers TAG synthesis in yeast H1246, a TAG synthesis quadruple mutant (are1, are2, lro1, dga1). The mutant transformed with the empty vector served as negative control. The wild type is SCY62, and the right lane is the TAG standard. Triacylglycerols are boxed.

Mentions: To confirm the functionality of the four candidate enzymes, each of them were expressed in the quadruple mutant yeast strain H1246, mutated in all four TAG synthesis genes (are1, are2, lro1, and dga1), so that the strain synthesizes no TAG (Sandager et al., 2002). When expressed in this yeast mutant strain, each of the B. napus enzymes supported TAG synthesis (Fig. 4). These results encouraged the authors to proceed with a more detailed functional analysis of enzyme activities by assaying microsomal preparations from the mutant yeast expressing each of the four B. napus DGAT1 isoforms. For these assays, one of two DAG substrates were supplied, either palmitoyl/oleoyl DAG (1-palmitoyl-2-oleoyl-sn-glycerol, PO-DAG) or oleoyl/oleoyl DAG (1,2-dioleoyl-sn-glycerol, OO-DAG), appropriate physiological DAG substrates for TAG synthesis in B. napus seeds. For fatty acid substrates, [14C]-labelled palmitoyl-CoA (16:0-CoA) and [14C]-labelled oleoyl-CoA (18:1-CoA) were provided.


Type 1 diacylglycerol acyltransferases of Brassica napus preferentially incorporate oleic acid into triacylglycerol.

Aznar-Moreno J, Denolf P, Van Audenhove K, De Bodt S, Engelen S, Fahy D, Wallis JG, Browse J - J. Exp. Bot. (2015)

Separation of yeast lipids by TLC. Expression of each BnDGAT1 recovers TAG synthesis in yeast H1246, a TAG synthesis quadruple mutant (are1, are2, lro1, dga1). The mutant transformed with the empty vector served as negative control. The wild type is SCY62, and the right lane is the TAG standard. Triacylglycerols are boxed.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4588894&req=5

Figure 4: Separation of yeast lipids by TLC. Expression of each BnDGAT1 recovers TAG synthesis in yeast H1246, a TAG synthesis quadruple mutant (are1, are2, lro1, dga1). The mutant transformed with the empty vector served as negative control. The wild type is SCY62, and the right lane is the TAG standard. Triacylglycerols are boxed.
Mentions: To confirm the functionality of the four candidate enzymes, each of them were expressed in the quadruple mutant yeast strain H1246, mutated in all four TAG synthesis genes (are1, are2, lro1, and dga1), so that the strain synthesizes no TAG (Sandager et al., 2002). When expressed in this yeast mutant strain, each of the B. napus enzymes supported TAG synthesis (Fig. 4). These results encouraged the authors to proceed with a more detailed functional analysis of enzyme activities by assaying microsomal preparations from the mutant yeast expressing each of the four B. napus DGAT1 isoforms. For these assays, one of two DAG substrates were supplied, either palmitoyl/oleoyl DAG (1-palmitoyl-2-oleoyl-sn-glycerol, PO-DAG) or oleoyl/oleoyl DAG (1,2-dioleoyl-sn-glycerol, OO-DAG), appropriate physiological DAG substrates for TAG synthesis in B. napus seeds. For fatty acid substrates, [14C]-labelled palmitoyl-CoA (16:0-CoA) and [14C]-labelled oleoyl-CoA (18:1-CoA) were provided.

Bottom Line: Thorough understanding of the enzymology of oil accumulation is critical to the goal of modifying oilseeds for improved vegetable oil production.This strong sensitivity of the BnDGAT1 isozymes to the relative concentrations of acyl-CoA substrates substantially explains the observed fatty acid composition of B. napus seed oil.Understanding these enzymes that are critical for triacylglycerol synthesis will facilitate genetic and biotechnological manipulations to improve this oilseed crop.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340, USA.

No MeSH data available.


Related in: MedlinePlus