Plant Acyl-CoA:Lysophosphatidylcholine Acyltransferases (LPCATs) Have Different Specificities in Their Forward and Reverse Reactions

Lager, Ida; Yilmaz, Jenny Lindberg; Zhou, Xue-Rong; Jasieniecka, Katarzyna; Kazachkov, Michael; Wang, Peng; Zou, Jitao; Weselake, Randall J.; Smith, Mark A.; Bayon, Shen; Dyer, John M.; Shockey, Jay; Heinz, Ernst; Green, Allan; Banaś, Antoni; Stymne, Sten

doi:10.1074/jbc.m113.521815

Cited by 127 publications

(186 citation statements)

References 44 publications

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“…Taken together with earlier reported in vitro data on plant LPCAT action (13), our data further confirm that plant LPCAT can act in a reversible fashion under in vivo condition. These data demonstrate for the first time in vivo evidence of the reversibility of the LPCAT.…”

supporting

confidence: 78%

“…Recently, by using reverse genetics and metabolic labeling approaches, it was demonstrated that LPCAT-mediated acyl-editing together with phosphatidylcholine:diacylglycerol cholinephosphotransferase-based PC-sn-1,2-diacylglycerol interconversion control the major fluxes of PUFAs from PC to TAG (ϳ66%) in Arabidopsis seeds (12). In addition, in vitro evidence has shown that plant LPCAT does indeed operate in a reversible fashion, even though the reverse reaction is a thermodynamically unfavorable process (13). Despite recent progress, direct evidence of how LPCAT interacts with the enzymes involved in the Kennedy pathway is still lacking.…”

mentioning

confidence: 99%

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In Vivo and in Vitro Evidence for Biochemical Coupling of Reactions Catalyzed by Lysophosphatidylcholine Acyltransferase and Diacylglycerol Acyltransferase

Pan

Chen

Kazachkov

et al. 2015

Journal of Biological Chemistry

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Background: Plant polyunsaturated fatty acids (PUFAs) are mainly synthesized on phosphatidylcholine (PC). Results: Diacylglycerol acyltransferase (DGAT) produced higher amount of PUFA-containing TAG in the presence of acylCoA:lysophosphatidylcholine acyltransferase (LPCAT). Conclusion:The LPCAT-catalyzed reverse reaction can be coupled to the DGAT reaction for PUFA accumulation. Significance: A mechanism for enhancing the transfer of PUFAs from PC into TAG has been confirmed.

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confidence: 78%

mentioning

confidence: 99%

In Vivo and in Vitro Evidence for Biochemical Coupling of Reactions Catalyzed by Lysophosphatidylcholine Acyltransferase and Diacylglycerol Acyltransferase

Pan

Chen

Kazachkov

et al. 2015

Journal of Biological Chemistry

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“…3A). However, this loss of oleate from PC through the preferential hydrolysis of 18:1-PC over sn-1-palmitoylsn-2-ricinoleoylphosphatidylcholine (Ric-PC) may be mitigated to some extent through the selective reacylation of LPC by the endogenous Arabidopsis LPCATs (Lager et al, 2013). The newly liberated oleic acid would have to be reactivated to its CoA-thioester, prior to transfer catalyzed by LPCAT into PC, via the catalytic action of long-chain acyl-coenzyme A synthetase (LACS; Shockey et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

“…As suggested by Lands (1960), PC deacylation was initially thought to result from the activity of a phospholipase. Until now, in plants, however, evidence suggested that LPC production comes from the action of phospholipid:diacylglycerol acyltransferase (PDAT; Zhang et al, 2009;van Erp et al, 2011;Xu et al, 2012) and through the reverse activity of LPCAT (Stymne and Stobart, 1984;Yurchenko et al, 2009;Lager et al, 2013). Thus, acyl editing includes a broader set of enzymatic activities than originally envisioned by Lands (1960).…”

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confidence: 93%

A Small Phospholipase A2-α from Castor Catalyzes the Removal of Hydroxy Fatty Acids from Phosphatidylcholine in Transgenic Arabidopsis Seeds

et al. 2015

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Ricinoleic acid, an industrially useful hydroxy fatty acid (HFA), only accumulates to high levels in the triacylglycerol fraction of castor (Ricinus communis) endosperm, even though it is synthesized on the membrane lipid phosphatidylcholine (PC) from an oleoyl ester. The acyl chains of PC undergo intense remodeling through the process of acyl editing. The identities of the proteins involved in this process, however, are unknown. A phospholipase A2 (PLA2) is thought to be involved in the acyl-editing process. We show here a role for RcsPLA2α in the acyl editing of HFA esterified to PC. RcsPLA2α was identified by its high relative expression in the castor endosperm transcriptome. Coexpression in Arabidopsis (Arabidopsis thaliana) seeds of RcsPLA2α with the castor fatty acid hydroxylase RcFAH12 led to a dramatic decrease in seed HFA content when compared with RcFAH12 expression alone in both PC and the neutral lipid fraction. The low-HFA trait was heritable and gene dosage dependent, with hemizygous lines showing intermediate HFA levels. The low seed HFA levels suggested that RcsPLA2α functions in vivo as a PLA2 with HFA specificity. Activity assays with yeast (Saccharomyces cerevisiae) microsomes showed a high specificity of RcsPLA2α for ricinoleic acid, superior to that of the endogenous Arabidopsis PLA2α. These results point to RcsPLA2α as a phospholipase involved in acyl editing, adapted to specifically removing HFA from membrane lipids in seeds.

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“…Acyl groups esterified to PC become substrates for FA desaturation and other modifications (Miquel and Browse, 1992;Broun et al, 1998) and can then be returned back to the acyl-CoA pool or channeled into TAG through acylCoA-independent mechanisms (Stymne and Stobart, 1984;Weselake, 2005;Lager et al, 2013). The efficiency of this acyl group channeling to and from PC is an important determinant of the overall composition of FAs in the acyl-CoA pool and, subsequently, in seed oil.…”

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confidence: 99%

Production of a Brassica napus Low-Molecular Mass Acyl-Coenzyme A-Binding Protein in Arabidopsis Alters the Acyl-Coenzyme A Pool and Acyl Composition of Oil in Seeds

et al. 2014

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Low-molecular mass (10 kD) cytosolic acyl-coenzyme A-binding protein (ACBP) has a substantial influence over fatty acid (FA) composition in oilseeds, possibly via an effect on the partitioning of acyl groups between elongation and desaturation pathways. Previously, we demonstrated that the expression of a Brassica napus ACBP (BnACBP) complementary DNA in the developing seeds of Arabidopsis (Arabidopsis thaliana) resulted in increased levels of polyunsaturated FAs at the expense of eicosenoic acid (20:1 cisD11 ) and saturated FAs in seed oil. In this study, we investigated whether alterations in the FA composition of seed oil at maturity were correlated with changes in the acyl-coenzyme A (CoA) pool in developing seeds of transgenic Arabidopsis expressing BnACBP. Our results indicated that both the acyl-CoA pool and seed oil of transgenic Arabidopsis lines expressing cytosolic BnACBP exhibited relative increases in linoleic acid (18:2 cisD9,12 ; 17.9%-44.4% and 7%-13.2%, respectively) and decreases in 20:1 cisD11 (38.7%-60.7% and 13.8%-16.3%, respectively). However, alterations in the FA composition of the acylCoA pool did not always correlate with those seen in the seed oil. In addition, we found that targeting of BnACBP to the endoplasmic reticulum resulted in FA compositional changes that were similar to those seen in lines expressing cytosolic BnACBP, with the most prominent exception being a relative reduction in a-linolenic acid (18:3 cisD9,12,15 ) in both the acyl-CoA pool and seed oil of the former (48.4%-48.9% and 5.3%-10.4%, respectively). Overall, these data support the role of ACBP in acyl trafficking in developing seeds and validate its use as a biotechnological tool for modifying the FA composition of seed oil.

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Plant Acyl-CoA:Lysophosphatidylcholine Acyltransferases (LPCATs) Have Different Specificities in Their Forward and Reverse Reactions

Cited by 127 publications

References 44 publications

In Vivo and in Vitro Evidence for Biochemical Coupling of Reactions Catalyzed by Lysophosphatidylcholine Acyltransferase and Diacylglycerol Acyltransferase

In Vivo and in Vitro Evidence for Biochemical Coupling of Reactions Catalyzed by Lysophosphatidylcholine Acyltransferase and Diacylglycerol Acyltransferase

A Small Phospholipase A2-α from Castor Catalyzes the Removal of Hydroxy Fatty Acids from Phosphatidylcholine in Transgenic Arabidopsis Seeds

Production of a Brassica napus Low-Molecular Mass Acyl-Coenzyme A-Binding Protein in Arabidopsis Alters the Acyl-Coenzyme A Pool and Acyl Composition of Oil in Seeds

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