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A small phospholipase A2-α from castor catalyzes the removal of hydroxy fatty acids from phosphatidylcholine in transgenic Arabidopsis seeds.
Plant Physiol. 2015 Apr; 167(4):1259-70.PP

Abstract

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.

Authors+Show Affiliations

Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340 (S.B., J.B.); andAlberta Innovates Phytola Centre, Department of Agricultural, Food, and Nutritional Science, University of Alberta, Edmonton, Alberta, Canada T6G 2P5 (G.C., R.J.W.).Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340 (S.B., J.B.); andAlberta Innovates Phytola Centre, Department of Agricultural, Food, and Nutritional Science, University of Alberta, Edmonton, Alberta, Canada T6G 2P5 (G.C., R.J.W.).Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340 (S.B., J.B.); andAlberta Innovates Phytola Centre, Department of Agricultural, Food, and Nutritional Science, University of Alberta, Edmonton, Alberta, Canada T6G 2P5 (G.C., R.J.W.).Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340 (S.B., J.B.); andAlberta Innovates Phytola Centre, Department of Agricultural, Food, and Nutritional Science, University of Alberta, Edmonton, Alberta, Canada T6G 2P5 (G.C., R.J.W.) jab@wsu.edu.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

25667315

Citation

Bayon, Shen, et al. "A Small Phospholipase A2-α From Castor Catalyzes the Removal of Hydroxy Fatty Acids From Phosphatidylcholine in Transgenic Arabidopsis Seeds." Plant Physiology, vol. 167, no. 4, 2015, pp. 1259-70.
Bayon S, Chen G, Weselake RJ, et al. A small phospholipase A2-α from castor catalyzes the removal of hydroxy fatty acids from phosphatidylcholine in transgenic Arabidopsis seeds. Plant Physiol. 2015;167(4):1259-70.
Bayon, S., Chen, G., Weselake, R. J., & Browse, J. (2015). A small phospholipase A2-α from castor catalyzes the removal of hydroxy fatty acids from phosphatidylcholine in transgenic Arabidopsis seeds. Plant Physiology, 167(4), 1259-70. https://doi.org/10.1104/pp.114.253641
Bayon S, et al. A Small Phospholipase A2-α From Castor Catalyzes the Removal of Hydroxy Fatty Acids From Phosphatidylcholine in Transgenic Arabidopsis Seeds. Plant Physiol. 2015;167(4):1259-70. PubMed PMID: 25667315.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A small phospholipase A2-α from castor catalyzes the removal of hydroxy fatty acids from phosphatidylcholine in transgenic Arabidopsis seeds. AU - Bayon,Shen, AU - Chen,Guanqun, AU - Weselake,Randall J, AU - Browse,John, Y1 - 2015/02/09/ PY - 2015/2/11/entrez PY - 2015/2/11/pubmed PY - 2016/2/10/medline SP - 1259 EP - 70 JF - Plant physiology JO - Plant Physiol VL - 167 IS - 4 N2 - 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. SN - 1532-2548 UR - https://www.unboundmedicine.com/medline/citation/25667315/A_small_phospholipase_A2_α_from_castor_catalyzes_the_removal_of_hydroxy_fatty_acids_from_phosphatidylcholine_in_transgenic_Arabidopsis_seeds_ L2 - http://www.plantphysiol.org/lookup/pmidlookup?view=long&pmid=25667315 DB - PRIME DP - Unbound Medicine ER -