Cloning of glycerophosphocholine acyltransferase (GPCAT) from fungi and plants : A novel enzyme in phosphatidylcholine synthesis
(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
- Głab, Bartosz ; Beganovic, Mirela ; Anaokar, Sanket ; Hao, Mengshu LU ; Rasmusson, Allan G. LU ; Patton-Vogt, Jana ; Banaś, Antoni ; Stymne, Sten and Lager, Ida LU
- organization
- publishing date
- 2016-11-25
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 291
- issue
- 48
- pages
- 11 pages
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:27758859
- wos:000388880100022
- scopus:84997606226
- 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
- 2024-10-05 07:51:40
@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 = {{American Society for Biochemistry and Molecular Biology}},
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}},
doi = {{10.1074/jbc.M116.743062}},
volume = {{291}},
year = {{2016}},
}