title: Cloning of Glycerophosphocholine Acyltransferase (GPCAT) from Fungi and Plants: A NOVEL ENZYME IN PHOSPHATIDYLCHOLINE SYNTHESIS.
abstract: Glycero-3-phosphocholine (GPC), the product of the complete deacylation of phosphatidylcholine (PC), was long thought to not be a substrate for reacylation. However, it was recently shown that cell-free extracts from yeast and plants could acylate GPC with acyl groups from acyl-CoA. By screening enzyme activities of extracts derived from a yeast knock-out collection, we were able to identify and clone the yeast gene (GPC1) encoding the enzyme, named glycerophosphocholine acyltransferase (GPCAT). By homology search, we also identified and cloned GPCAT genes from three plant species. All enzymes utilize acyl-CoA to acylate GPC, forming lyso-PC, and they show broad acyl specificities in both yeast and plants. In addition to acyl-CoA, GPCAT efficiently utilizes LPC and lysophosphatidylethanolamine as acyl donors in the acylation of GPC. GPCAT homologues were found in the major eukaryotic organism groups but not in prokaryotes or chordates. The enzyme forms its own protein family and does not contain any of the acyl binding or lipase motifs that are present in other studied acyltransferases and transacylases. In vivo labeling studies confirm a role for Gpc1p in PC biosynthesis in yeast. It is postulated that GPCATs contribute to the maintenance of PC homeostasis and also have specific functions in acyl editing of PC (e.g. in transferring acyl groups modified at the sn-2 position of PC to the sn-1 position of this molecule in plant cells).
authors.affiliation: From the Intercollegiate Faculty of Biotechnology, University of Gdańsk and Medical University of Gdańsk, 80-822 Gdańsk, Poland.
authors.forename: Bartosz
authors.initials: B
authors.lastname: Głąb
authors.affiliation: the Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53 Alnarp, Sweden.
authors.forename: Mirela
authors.initials: M
authors.lastname: Beganovic
authors.affiliation: the Department of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, and.
authors.forename: Sanket
authors.initials: S
authors.lastname: Anaokar
authors.affiliation: the Department of Biology, Lund University, Biology Building A, Sölvegatan 35, 223 62 Lund, Sweden.
authors.forename: Meng-Shu
authors.initials: MS
authors.lastname: Hao
authors.affiliation: the Department of Biology, Lund University, Biology Building A, Sölvegatan 35, 223 62 Lund, Sweden.
authors.forename: Allan G
authors.initials: AG
authors.lastname: Rasmusson
authors.affiliation: the Department of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, and.
authors.forename: Jana
authors.initials: J
authors.lastname: Patton-Vogt
authors.affiliation: From the Intercollegiate Faculty of Biotechnology, University of Gdańsk and Medical University of Gdańsk, 80-822 Gdańsk, Poland.
authors.forename: Antoni
authors.initials: A
authors.lastname: Banaś
authors.affiliation: the Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53 Alnarp, Sweden.
authors.forename: Sten
authors.initials: S
authors.lastname: Stymne
authors.affiliation: the Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53 Alnarp, Sweden, ida.lager@slu.se.
authors.forename: Ida
authors.identifier: http://orcid.org/0000-0001-9755-8534
authors.initials: I
authors.lastname: Lager
mesh_terms: D000214:Acyl Coenzyme A / Q000235:genetics / Q000378:metabolism; D000215:Acylation; D000217:Acyltransferases / Q000235:genetics / Q000378:metabolism*; D010713:Phosphatidylcholines / Q000096:biosynthesis* / Q000235:genetics; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D010944:Plants / Q000201:enzymology* / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D000214:Acyl Coenzyme A; D010713:Phosphatidylcholines; D010940:Plant Proteins; D029701:Saccharomyces cerevisiae Proteins; D000217:Acyltransferases; C531220:glycerophosphocholine acyltransferase, S cerevisiae
keywords: acyltransferase; glycerophospholipid; lipid metabolism; phosphatidylcholine; plant biochemistry