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Physaria fendleri and Ricinus communis lecithin:cholesterol acyltransferase-like phospholipases selectively cleave hydroxy acyl chains from phosphatidylcholine.
Plant J. 2021 01; 105(1):182-196.PJ

Abstract

Production of hydroxy fatty acids (HFAs) in transgenic crops represents a promising strategy to meet our demands for specialized plant oils with industrial applications. The expression of Ricinus communis (castor) OLEATE 12-HYDROXYLASE (RcFAH12) in Arabidopsis has resulted in only limited accumulation of HFAs in seeds, which probably results from inefficient transfer of HFAs from their site of synthesis (phosphatidylcholine; PC) to triacylglycerol (TAG), especially at the sn-1/3 positions of TAG. Phospholipase As (PLAs) may be directly involved in the liberation of HFAs from PC, but the functions of their over-expression in HFA accumulation and distribution at TAG in transgenic plants have not been well studied. In this work, the functions of lecithin:cholesterol acyltransferase-like PLAs (LCAT-PLAs) in HFA biosynthesis were characterized. The LCAT-PLAs were shown to exhibit homology to LCAT and mammalian lysosomal PLA2 , and to contain a conserved and functional Ser/His/Asp catalytic triad. In vitro assays revealed that LCAT-PLAs from the HFA-accumulating plant species Physaria fendleri (PfLCAT-PLA) and castor (RcLCAT-PLA) could cleave acyl chains at both the sn-1 and sn-2 positions of PC, and displayed substrate selectivity towards sn-2-ricinoleoyl-PC over sn-2-oleoyl-PC. Furthermore, co-expression of RcFAH12 with PfLCAT-PLA or RcLCAT-PLA, but not Arabidopsis AtLCAT-PLA, resulted in increased occupation of HFA at the sn-1/3 positions of TAG as well as small but insignificant increases in HFA levels in Arabidopsis seeds compared with RcFAH12 expression alone. Therefore, PfLCAT-PLA and RcLCAT-PLA may contribute to HFA turnover on PC, and represent potential candidates for engineering the production of unusual fatty acids in crops.

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Authors+Show Affiliations

Xu Y
Department of Agricultural, Food and Nutritional Science, 410 Agriculture/Forestry Centre, University of Alberta, Edmonton, Alberta, T6G 2P5, Canada.
Caldo KMP
Department of Agricultural, Food and Nutritional Science, 410 Agriculture/Forestry Centre, University of Alberta, Edmonton, Alberta, T6G 2P5, Canada.
Singer SD
Department of Agricultural, Food and Nutritional Science, 410 Agriculture/Forestry Centre, University of Alberta, Edmonton, Alberta, T6G 2P5, Canada. Agriculture and Agri-Food Canada, Lethbridge Research and Development Centre, Lethbridge, Alberta, T1J 4B1, Canada.
Mietkiewska E
Department of Agricultural, Food and Nutritional Science, 410 Agriculture/Forestry Centre, University of Alberta, Edmonton, Alberta, T6G 2P5, Canada.
Greer MS
Department of Agricultural, Food and Nutritional Science, 410 Agriculture/Forestry Centre, University of Alberta, Edmonton, Alberta, T6G 2P5, Canada.
Tian B
Department of Agricultural, Food and Nutritional Science, 410 Agriculture/Forestry Centre, University of Alberta, Edmonton, Alberta, T6G 2P5, Canada. CAS Key Laboratory of Tropical Plant Resource and Sustainable Use, Xishuangbanna Tropical Botanical Garden, Chinese Academy of Sciences, Kunming, 650223, China.
Dyer JM
U.S. Department of Agriculture-Agricultural Research Service, US Arid-Land Agricultural Research Center, Maricopa, AZ, 85138, USA.
Smith M
Agriculture and Agri-Food Canada, 107 Science Place, Saskatoon, Saskatchewan, S7N 0X2, Canada.
Zhou XR
CSIRO Agriculture and Food, PO Box 1700, Canberra, ACT, 2601, Australia.
Qiu X
Department of Food and Bioproduct Sciences, University of Saskatchewan, Saskatoon, Saskatchewan, S7N 5A8, Canada.
Weselake RJ
Department of Agricultural, Food and Nutritional Science, 410 Agriculture/Forestry Centre, University of Alberta, Edmonton, Alberta, T6G 2P5, Canada.
Chen G
Department of Agricultural, Food and Nutritional Science, 410 Agriculture/Forestry Centre, University of Alberta, Edmonton, Alberta, T6G 2P5, Canada.

MeSH

ArabidopsisBrassicaceaeFatty AcidsLysophospholipidsPhosphatidylcholine-Sterol O-AcyltransferasePhosphatidylcholinesPlant ProteinsPlant RootsPlants, Genetically ModifiedProtein Structure, TertiaryRicinusSeedsSubstrate Specificity

Pub Type(s)

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

Language

eng

PubMed ID

33107656

Citation

Xu, Yang, et al. "Physaria Fendleri and Ricinus Communis Lecithin:cholesterol Acyltransferase-like Phospholipases Selectively Cleave Hydroxy Acyl Chains From Phosphatidylcholine." The Plant Journal : for Cell and Molecular Biology, vol. 105, no. 1, 2021, pp. 182-196.
Xu Y, Caldo KMP, Singer SD, et al. Physaria fendleri and Ricinus communis lecithin:cholesterol acyltransferase-like phospholipases selectively cleave hydroxy acyl chains from phosphatidylcholine. Plant J. 2021;105(1):182-196.
Xu, Y., Caldo, K. M. P., Singer, S. D., Mietkiewska, E., Greer, M. S., Tian, B., Dyer, J. M., Smith, M., Zhou, X. R., Qiu, X., Weselake, R. J., & Chen, G. (2021). Physaria fendleri and Ricinus communis lecithin:cholesterol acyltransferase-like phospholipases selectively cleave hydroxy acyl chains from phosphatidylcholine. The Plant Journal : for Cell and Molecular Biology, 105(1), 182-196. https://doi.org/10.1111/tpj.15050
Xu Y, et al. Physaria Fendleri and Ricinus Communis Lecithin:cholesterol Acyltransferase-like Phospholipases Selectively Cleave Hydroxy Acyl Chains From Phosphatidylcholine. Plant J. 2021;105(1):182-196. PubMed PMID: 33107656.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Physaria fendleri and Ricinus communis lecithin:cholesterol acyltransferase-like phospholipases selectively cleave hydroxy acyl chains from phosphatidylcholine. AU - Xu,Yang, AU - Caldo,Kristian Mark P, AU - Singer,Stacy D, AU - Mietkiewska,Elzbieta, AU - Greer,Michael S, AU - Tian,Bo, AU - Dyer,John M, AU - Smith,Mark, AU - Zhou,Xue-Rong, AU - Qiu,Xiao, AU - Weselake,Randall J, AU - Chen,Guanqun, Y1 - 2020/11/27/ PY - 2020/07/10/received PY - 2020/10/12/revised PY - 2020/10/21/accepted PY - 2020/10/28/pubmed PY - 2021/6/10/medline PY - 2020/10/27/entrez KW - Arabidopsis thaliana KW - Physaria fendleri KW - Ricinus communis KW - hydroxy fatty acid KW - lecithin:cholesterol acyltransferase-like PLA KW - phosphatidylcholine KW - phospholipase A KW - triacylglycerol SP - 182 EP - 196 JF - The Plant journal : for cell and molecular biology JO - Plant J VL - 105 IS - 1 N2 - Production of hydroxy fatty acids (HFAs) in transgenic crops represents a promising strategy to meet our demands for specialized plant oils with industrial applications. The expression of Ricinus communis (castor) OLEATE 12-HYDROXYLASE (RcFAH12) in Arabidopsis has resulted in only limited accumulation of HFAs in seeds, which probably results from inefficient transfer of HFAs from their site of synthesis (phosphatidylcholine; PC) to triacylglycerol (TAG), especially at the sn-1/3 positions of TAG. Phospholipase As (PLAs) may be directly involved in the liberation of HFAs from PC, but the functions of their over-expression in HFA accumulation and distribution at TAG in transgenic plants have not been well studied. In this work, the functions of lecithin:cholesterol acyltransferase-like PLAs (LCAT-PLAs) in HFA biosynthesis were characterized. The LCAT-PLAs were shown to exhibit homology to LCAT and mammalian lysosomal PLA2 , and to contain a conserved and functional Ser/His/Asp catalytic triad. In vitro assays revealed that LCAT-PLAs from the HFA-accumulating plant species Physaria fendleri (PfLCAT-PLA) and castor (RcLCAT-PLA) could cleave acyl chains at both the sn-1 and sn-2 positions of PC, and displayed substrate selectivity towards sn-2-ricinoleoyl-PC over sn-2-oleoyl-PC. Furthermore, co-expression of RcFAH12 with PfLCAT-PLA or RcLCAT-PLA, but not Arabidopsis AtLCAT-PLA, resulted in increased occupation of HFA at the sn-1/3 positions of TAG as well as small but insignificant increases in HFA levels in Arabidopsis seeds compared with RcFAH12 expression alone. Therefore, PfLCAT-PLA and RcLCAT-PLA may contribute to HFA turnover on PC, and represent potential candidates for engineering the production of unusual fatty acids in crops. SN - 1365-313X UR - https://www.unboundmedicine.com/medline/citation/33107656/Physaria_fendleri_and_Ricinus_communis_lecithin:cholesterol_acyltransferase_like_phospholipases_selectively_cleave_hydroxy_acyl_chains_from_phosphatidylcholine_ L2 - https://doi.org/10.1111/tpj.15050 DB - PRIME DP - Unbound Medicine ER -