Functional analysis of alternative castor bean DGAT enzymes

Detalhes bibliográficos
Autor(a) principal: Trenz,Thomaz Stumpf
Data de Publicação: 2023
Outros Autores: Turchetto-Zolet,Andreia Carina, Margis,Rogério, Margis-Pinheiro,Marcia, Maraschin,Felipe dos Santos
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Genetics and Molecular Biology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572023000200101
Resumo: Abstract The diversity of diacylglycerol acyltransferases (DGATs) indicates alternative roles for these enzymes in plant metabolism besides triacylglycerol (TAG) biosynthesis. In this work, we functionally characterized castor bean (Ricinus communis L.) DGATs assessing their subcellular localization, expression in seeds, capacity to restore triacylglycerol (TAG) biosynthesis in mutant yeast and evaluating whether they provide tolerance over free fatty acids (FFA) in sensitive yeast. RcDGAT3 displayed a distinct subcellular localization, located in vesicles outside the endoplasmic reticulum (ER) in most leaf epidermal cells. This enzyme was unable to restore TAG biosynthesis in mutant yeast; however, it was able to outperform other DGATs providing higher tolerance over FFA. RcDAcTA subcellular localization was associated with the ER membranes, resembling RcDGAT1 and RcDGAT2, but it failed to rescue the long-chain TAG biosynthesis in mutant yeast, even with fatty acid supplementation. Besides TAG biosynthesis, our results suggest that RcDGAT3 might have alternative functions and roles in lipid metabolism.
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spelling Functional analysis of alternative castor bean DGAT enzymesTAGlipidsoildiacylglycerol acyltransferaseRicinusAbstract The diversity of diacylglycerol acyltransferases (DGATs) indicates alternative roles for these enzymes in plant metabolism besides triacylglycerol (TAG) biosynthesis. In this work, we functionally characterized castor bean (Ricinus communis L.) DGATs assessing their subcellular localization, expression in seeds, capacity to restore triacylglycerol (TAG) biosynthesis in mutant yeast and evaluating whether they provide tolerance over free fatty acids (FFA) in sensitive yeast. RcDGAT3 displayed a distinct subcellular localization, located in vesicles outside the endoplasmic reticulum (ER) in most leaf epidermal cells. This enzyme was unable to restore TAG biosynthesis in mutant yeast; however, it was able to outperform other DGATs providing higher tolerance over FFA. RcDAcTA subcellular localization was associated with the ER membranes, resembling RcDGAT1 and RcDGAT2, but it failed to rescue the long-chain TAG biosynthesis in mutant yeast, even with fatty acid supplementation. Besides TAG biosynthesis, our results suggest that RcDGAT3 might have alternative functions and roles in lipid metabolism.Sociedade Brasileira de Genética2023-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572023000200101Genetics and Molecular Biology v.46 n.1 suppl.1 2023reponame:Genetics and Molecular Biologyinstname:Sociedade Brasileira de Genética (SBG)instacron:SBG10.1590/1678-4685-gmb-2022-0097info:eu-repo/semantics/openAccessTrenz,Thomaz StumpfTurchetto-Zolet,Andreia CarinaMargis,RogérioMargis-Pinheiro,MarciaMaraschin,Felipe dos Santoseng2022-12-06T00:00:00Zoai:scielo:S1415-47572023000200101Revistahttp://www.gmb.org.br/ONGhttps://old.scielo.br/oai/scielo-oai.php||editor@gmb.org.br1678-46851415-4757opendoar:2022-12-06T00:00Genetics and Molecular Biology - Sociedade Brasileira de Genética (SBG)false
dc.title.none.fl_str_mv Functional analysis of alternative castor bean DGAT enzymes
title Functional analysis of alternative castor bean DGAT enzymes
spellingShingle Functional analysis of alternative castor bean DGAT enzymes
Trenz,Thomaz Stumpf
TAG
lipids
oil
diacylglycerol acyltransferase
Ricinus
title_short Functional analysis of alternative castor bean DGAT enzymes
title_full Functional analysis of alternative castor bean DGAT enzymes
title_fullStr Functional analysis of alternative castor bean DGAT enzymes
title_full_unstemmed Functional analysis of alternative castor bean DGAT enzymes
title_sort Functional analysis of alternative castor bean DGAT enzymes
author Trenz,Thomaz Stumpf
author_facet Trenz,Thomaz Stumpf
Turchetto-Zolet,Andreia Carina
Margis,Rogério
Margis-Pinheiro,Marcia
Maraschin,Felipe dos Santos
author_role author
author2 Turchetto-Zolet,Andreia Carina
Margis,Rogério
Margis-Pinheiro,Marcia
Maraschin,Felipe dos Santos
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Trenz,Thomaz Stumpf
Turchetto-Zolet,Andreia Carina
Margis,Rogério
Margis-Pinheiro,Marcia
Maraschin,Felipe dos Santos
dc.subject.por.fl_str_mv TAG
lipids
oil
diacylglycerol acyltransferase
Ricinus
topic TAG
lipids
oil
diacylglycerol acyltransferase
Ricinus
description Abstract The diversity of diacylglycerol acyltransferases (DGATs) indicates alternative roles for these enzymes in plant metabolism besides triacylglycerol (TAG) biosynthesis. In this work, we functionally characterized castor bean (Ricinus communis L.) DGATs assessing their subcellular localization, expression in seeds, capacity to restore triacylglycerol (TAG) biosynthesis in mutant yeast and evaluating whether they provide tolerance over free fatty acids (FFA) in sensitive yeast. RcDGAT3 displayed a distinct subcellular localization, located in vesicles outside the endoplasmic reticulum (ER) in most leaf epidermal cells. This enzyme was unable to restore TAG biosynthesis in mutant yeast; however, it was able to outperform other DGATs providing higher tolerance over FFA. RcDAcTA subcellular localization was associated with the ER membranes, resembling RcDGAT1 and RcDGAT2, but it failed to rescue the long-chain TAG biosynthesis in mutant yeast, even with fatty acid supplementation. Besides TAG biosynthesis, our results suggest that RcDGAT3 might have alternative functions and roles in lipid metabolism.
publishDate 2023
dc.date.none.fl_str_mv 2023-01-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572023000200101
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572023000200101
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/1678-4685-gmb-2022-0097
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Sociedade Brasileira de Genética
publisher.none.fl_str_mv Sociedade Brasileira de Genética
dc.source.none.fl_str_mv Genetics and Molecular Biology v.46 n.1 suppl.1 2023
reponame:Genetics and Molecular Biology
instname:Sociedade Brasileira de Genética (SBG)
instacron:SBG
instname_str Sociedade Brasileira de Genética (SBG)
instacron_str SBG
institution SBG
reponame_str Genetics and Molecular Biology
collection Genetics and Molecular Biology
repository.name.fl_str_mv Genetics and Molecular Biology - Sociedade Brasileira de Genética (SBG)
repository.mail.fl_str_mv ||editor@gmb.org.br
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