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Cloning of Glycerophosphocholine Acyltransferase (GPCAT) from Fungi and Plants A NOVEL ENZYME IN PHOSPHATIDYLCHOLINE SYNTHESIS
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- Glab, Bartosz (author)
- Univ Gdansk, Intercollegiate Fac Biotechnol, PL-80822 Gdansk, Poland.;Med Univ Gdansk, PL-80822 Gdansk, Poland.,University of Gdansk,Medical University of Gdansk
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- Beganovic, Mirela (author)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för växtförädling,Department of Plant Breeding,Swedish Univ Agr Sci, Dept Plant Breeding, S-23053 Alnarp, Sweden.
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- Anaokar, Sanket (author)
- Duquesne Univ, Dept Biol Sci, Pittsburgh, PA 15282 USA.,Duquesne University
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- Univ Gdansk, Intercollegiate Fac Biotechnol, PL-80822 Gdansk, Poland;Med Univ Gdansk, PL-80822 Gdansk, Poland. University of Gdansk (creator_code:org_t)
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2016
- 2016
- English.
- In: Journal of Biological Chemistry. - : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC. - 0021-9258 .- 1083-351X. ; 291:48, s. 25066-25076
- Journal article (peer-reviewed)
Abstract
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- 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).
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
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