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Genome-wide analysis of the Glycerol-3-Phosphate Acyltransferase (GPAT) gene family reveals the evolution and diversification of plant GPATs

sn-Glycerol-3-phosphate 1-O-acyltransferase (GPAT) is an important enzyme that catalyzes the transfer of an acyl group from acyl-CoA or acyl-ACP to the sn-1 or sn-2 position of sn-glycerol-3-phosphate (G3P) to generate lysophosphatidic acids (LPAs). The functional studies of GPAT in plants demonstra...

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Autores principales: Waschburger, Edgar, Kulcheski, Franceli Rodrigues, Veto, Nicole Moreira, Margis, Rogerio, Margis-Pinheiro, Marcia, Turchetto-Zolet, Andreia Carina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Sociedade Brasileira de Genética 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5913721/
https://www.ncbi.nlm.nih.gov/pubmed/29583156
http://dx.doi.org/10.1590/1678-4685-GMB-2017-0076
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author Waschburger, Edgar
Kulcheski, Franceli Rodrigues
Veto, Nicole Moreira
Margis, Rogerio
Margis-Pinheiro, Marcia
Turchetto-Zolet, Andreia Carina
author_facet Waschburger, Edgar
Kulcheski, Franceli Rodrigues
Veto, Nicole Moreira
Margis, Rogerio
Margis-Pinheiro, Marcia
Turchetto-Zolet, Andreia Carina
author_sort Waschburger, Edgar
collection PubMed
description sn-Glycerol-3-phosphate 1-O-acyltransferase (GPAT) is an important enzyme that catalyzes the transfer of an acyl group from acyl-CoA or acyl-ACP to the sn-1 or sn-2 position of sn-glycerol-3-phosphate (G3P) to generate lysophosphatidic acids (LPAs). The functional studies of GPAT in plants demonstrated its importance in controlling storage and membrane lipid. Identifying genes encoding GPAT in a variety of plant species is crucial to understand their involvement in different metabolic pathways and physiological functions. Here, we performed genome-wide and evolutionary analyses of GPATs in plants. GPAT genes were identified in all algae and plants studied. The phylogenetic analysis showed that these genes group into three main clades. While clades I (GPAT9) and II (soluble GPAT) include GPATs from algae and plants, clade III (GPAT1-8) includes GPATs specific from plants that are involved in the biosynthesis of cutin or suberin. Gene organization and the expression pattern of GPATs in plants corroborate with clade formation in the phylogeny, suggesting that the evolutionary patterns is reflected in their functionality. Overall, our results provide important insights into the evolution of the plant GPATs and allowed us to explore the evolutionary mechanism underlying the functional diversification among these genes.
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spelling pubmed-59137212018-05-04 Genome-wide analysis of the Glycerol-3-Phosphate Acyltransferase (GPAT) gene family reveals the evolution and diversification of plant GPATs Waschburger, Edgar Kulcheski, Franceli Rodrigues Veto, Nicole Moreira Margis, Rogerio Margis-Pinheiro, Marcia Turchetto-Zolet, Andreia Carina Genet Mol Biol Research Articles sn-Glycerol-3-phosphate 1-O-acyltransferase (GPAT) is an important enzyme that catalyzes the transfer of an acyl group from acyl-CoA or acyl-ACP to the sn-1 or sn-2 position of sn-glycerol-3-phosphate (G3P) to generate lysophosphatidic acids (LPAs). The functional studies of GPAT in plants demonstrated its importance in controlling storage and membrane lipid. Identifying genes encoding GPAT in a variety of plant species is crucial to understand their involvement in different metabolic pathways and physiological functions. Here, we performed genome-wide and evolutionary analyses of GPATs in plants. GPAT genes were identified in all algae and plants studied. The phylogenetic analysis showed that these genes group into three main clades. While clades I (GPAT9) and II (soluble GPAT) include GPATs from algae and plants, clade III (GPAT1-8) includes GPATs specific from plants that are involved in the biosynthesis of cutin or suberin. Gene organization and the expression pattern of GPATs in plants corroborate with clade formation in the phylogeny, suggesting that the evolutionary patterns is reflected in their functionality. Overall, our results provide important insights into the evolution of the plant GPATs and allowed us to explore the evolutionary mechanism underlying the functional diversification among these genes. Sociedade Brasileira de Genética 2018-03-19 2018 /pmc/articles/PMC5913721/ /pubmed/29583156 http://dx.doi.org/10.1590/1678-4685-GMB-2017-0076 Text en Copyright © 2018, Sociedade Brasileira de Genética. https://creativecommons.org/licenses/by/4.0/ License information: This is an open-access article distributed under the terms of the Creative Commons Attribution License (type CC-BY), which permits unrestricted use, distribution and reproduction in any medium, provided the original article is properly cited.
spellingShingle Research Articles
Waschburger, Edgar
Kulcheski, Franceli Rodrigues
Veto, Nicole Moreira
Margis, Rogerio
Margis-Pinheiro, Marcia
Turchetto-Zolet, Andreia Carina
Genome-wide analysis of the Glycerol-3-Phosphate Acyltransferase (GPAT) gene family reveals the evolution and diversification of plant GPATs
title Genome-wide analysis of the Glycerol-3-Phosphate Acyltransferase (GPAT) gene family reveals the evolution and diversification of plant GPATs
title_full Genome-wide analysis of the Glycerol-3-Phosphate Acyltransferase (GPAT) gene family reveals the evolution and diversification of plant GPATs
title_fullStr Genome-wide analysis of the Glycerol-3-Phosphate Acyltransferase (GPAT) gene family reveals the evolution and diversification of plant GPATs
title_full_unstemmed Genome-wide analysis of the Glycerol-3-Phosphate Acyltransferase (GPAT) gene family reveals the evolution and diversification of plant GPATs
title_short Genome-wide analysis of the Glycerol-3-Phosphate Acyltransferase (GPAT) gene family reveals the evolution and diversification of plant GPATs
title_sort genome-wide analysis of the glycerol-3-phosphate acyltransferase (gpat) gene family reveals the evolution and diversification of plant gpats
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5913721/
https://www.ncbi.nlm.nih.gov/pubmed/29583156
http://dx.doi.org/10.1590/1678-4685-GMB-2017-0076
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