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Cloning of glycerophosphocholine acyltransferase (GPCAT) from fungi and plants : A novel enzyme in phosphatidylcholine synthesis

Głab, Bartosz; Beganovic, Mirela; Anaokar, Sanket; Hao, Mengshu LU ; Rasmusson, Allan G. LU ; Patton-Vogt, Jana; Banaś, Antoni; Stymne, Sten and Lager, Ida LU (2016) In Journal of Biological Chemistry 291(48). p.25066-25076
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... (More)

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).

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
291
issue
48
pages
11 pages
publisher
ASBMB
external identifiers
  • scopus:84997606226
  • wos:000388880100022
ISSN
0021-9258
DOI
10.1074/jbc.M116.743062
language
English
LU publication?
yes
id
fd2c9b8b-2ec9-435f-9a56-b2cfca415ca4
date added to LUP
2016-12-09 08:57:56
date last changed
2017-09-18 11:30:42
@article{fd2c9b8b-2ec9-435f-9a56-b2cfca415ca4,
  abstract     = {<p>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).</p>},
  author       = {Głab, Bartosz and Beganovic, Mirela and Anaokar, Sanket and Hao, Mengshu and Rasmusson, Allan G. and Patton-Vogt, Jana and Banaś, Antoni and Stymne, Sten and Lager, Ida},
  issn         = {0021-9258},
  language     = {eng},
  month        = {11},
  number       = {48},
  pages        = {25066--25076},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Cloning of glycerophosphocholine acyltransferase (GPCAT) from fungi and plants : A novel enzyme in phosphatidylcholine synthesis},
  url          = {http://dx.doi.org/10.1074/jbc.M116.743062},
  volume       = {291},
  year         = {2016},
}