caa a22 4500 606209697 CHVBK 20210128101029.0 cr unu---uuuuu 210128e20150201xx s 000 0 eng 10.1007/s00425-014-2184-1 doi (NATIONALLICENCE)springer-10.1007/s00425-014-2184-1 Novel reactions in acyl editing of phosphatidylcholine by lysophosphatidylcholine transacylase (LPCT) and acyl-CoA:glycerophosphocholine acyltransferase (GPCAT) activities in microsomal preparations of plant tissues [Elektronische Daten] [Ida Lager, Bartosz Glab, Lovisa Eriksson, Guanqun Chen, Antoni Banas, Sten Stymne] Main conclusion : Plants have lysophosphatidylcholine transacylase (LPCT) and acyl-CoA:glycerophosphocholine acyltransferase (GPCAT) activities. The combined action of LPCT and GPCAT provides a novel route of PC re-synthesis after its deacylation. Abstract: Phosphatidylcholine (PC) is the major lipid in eukaryotic membranes and has a central role in overall plant lipid metabolism. It is also the site of production of polyunsaturated fatty acids in plants. The recently discovered acyl-CoA:glycerophosphocholine acyltransferase (GPCAT) activity in yeast provides a novel route of re-synthesising PC via lysophosphatidylcholine (LPC) after its deacylation. This route does not require the degradation of the glycerophosphocholine (GPC) into free choline, the activation of choline to CDP-choline, nor the utilization of CDP-choline by the CDP-choline:diacylglycerol cholinephosphotransferase. We show here that GPCAT activities also are present in membrane preparations from developing oil seeds of safflower and other species as well as in membrane preparations of roots and leaves of Arabidopsis, indicating that GPCAT activity plays a ubiquitous role in plant lipid metabolism. The last step in formation of GPC, the substrate for GPCAT, is the deacylation of LPC. Microsomal membranes of developing safflower seeds utilized LPC in LPC:LPC transacylation reactions (LPCT activities) creating PC and GPC. The results demonstrate that safflower membranes have LPCT and GPCAT activities that represent novel reactions for PC acyl editing. The physiological relevance of these reactions probably has to await identification of the enzymes catalysing these reactions. The Author(s), 2014 Lipid biochemistry nationallicence Phosphatidylcholine metabolism nationallicence Glycerophosphocholine:acyl-CoA acyltransferase nationallicence Lysophosphatidylcholine transferase nationallicence PC : Phosphatidylcholine nationallicence GPCAT : Acyl-CoA:glycerophosphocholine acyltransferase nationallicence LPC : Lysophosphatidylcholine nationallicence GPC : Glycerophosphocholine nationallicence LPCT : Lysophosphatidylcholine transacylase nationallicence CPT : CDP-choline:diacylglycerol cholinephosphotransferase nationallicence PLA, PLB : Phospholipase A, B nationallicence TAG : Triacylglycerol nationallicence LPCAT : Acyl-CoA:lysophosphatidylcholine acyltransferase nationallicence PDAT : Phospholipid:diacylglycerol acyltransferase nationallicence 16:0 : Palmitic acid nationallicence 18:0 : Stearic acid nationallicence 18:1 : Oleic acid nationallicence 18:2 : Linoleic acid nationallicence 18:3 : Α-linolenic acid nationallicence PDCT : Phospholipid:diacylglycerol cholinephosphotransferase nationallicence FFA : Free fatty acid nationallicence DAG : Diacylglycerol nationallicence TLC : Thin layer chromatography nationallicence BSA : Bovine serum albumin nationallicence DTNB : Dithionitrobenzoic acid nationallicence Lager Ida Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53, Alnarp, Sweden aut Glab Bartosz Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53, Alnarp, Sweden aut Eriksson Lovisa Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53, Alnarp, Sweden aut Chen Guanqun Alberta Innovates Phytola Centre, Department of Agricultural, Food, and Nutritional Science, University of Alberta, T6G 2P5, Edmonton, AB, Canada aut Banas Antoni Intercollegiate Faculty of Biotechnology of University of Gdańsk and Medical University of Gdansk, 80-822, Gdańsk, Poland aut Stymne Sten Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53, Alnarp, Sweden aut Planta Springer Berlin Heidelberg 241/2(2015-02-01), 347-358 0032-0935 241:2<347 2015 241 425 https://doi.org/10.1007/s00425-014-2184-1 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00425-014-2184-1 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Lager Ida Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53, Alnarp, Sweden aut NATIONALLICENCE 700 1- Glab Bartosz Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53, Alnarp, Sweden aut NATIONALLICENCE 700 1- Eriksson Lovisa Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53, Alnarp, Sweden aut NATIONALLICENCE 700 1- Chen Guanqun Alberta Innovates Phytola Centre, Department of Agricultural, Food, and Nutritional Science, University of Alberta, T6G 2P5, Edmonton, AB, Canada aut NATIONALLICENCE 700 1- Banas Antoni Intercollegiate Faculty of Biotechnology of University of Gdańsk and Medical University of Gdansk, 80-822, Gdańsk, Poland aut NATIONALLICENCE 700 1- Stymne Sten Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53, Alnarp, Sweden aut NATIONALLICENCE 773 0- Planta Springer Berlin Heidelberg 241/2(2015-02-01), 347-358 0032-0935 241:2<347 2015 241 425