Function and localization of the Arabidopsis thaliana diacylglycerol acyltransferase DGAT2 expressed in yeast.

Diacylglycerol acyltransferases (DGATs) catalyze the final and only committed step of triacylglycerol synthesis. DGAT activity is rate limiting for triacylglycerol accumulation in mammals, plants and microbes. DGATs belong to three different evolutionary classes. In Arabidopsis thaliana, DGAT1, enco...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Laure Aymé, Sébastien Baud, Bertrand Dubreucq, Florent Joffre, Thierry Chardot
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/619dba49b04f40ab9206eba54ea9078c
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:619dba49b04f40ab9206eba54ea9078c
record_format	dspace
spelling	oai:doaj.org-article:619dba49b04f40ab9206eba54ea9078c2021-11-18T08:26:37ZFunction and localization of the Arabidopsis thaliana diacylglycerol acyltransferase DGAT2 expressed in yeast.1932-620310.1371/journal.pone.0092237https://doaj.org/article/619dba49b04f40ab9206eba54ea9078c2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24663078/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Diacylglycerol acyltransferases (DGATs) catalyze the final and only committed step of triacylglycerol synthesis. DGAT activity is rate limiting for triacylglycerol accumulation in mammals, plants and microbes. DGATs belong to three different evolutionary classes. In Arabidopsis thaliana, DGAT1, encoded by At2g19450, is the major DGAT enzyme involved in triacylglycerol accumulation in seeds. Until recently, the function of DGAT2 (At3g51520) has remained elusive. Previous attempts to characterize its enzymatic function by heterologous expression in yeast were unsuccessful. In the present report we demonstrate that expression of a codon-optimized version of the DGAT2 gene is able to restore neutral lipid accumulation in the Saccharomyces cerevisiae mutant strain (H1246), which is defective in triacylglycerol biosynthesis. Heterologous expression of codon-optimized DGAT2 and DGAT1 induced the biogenesis of subcellular lipid droplets containing triacylglycerols and squalene. Both DGAT proteins were found to be associated with these lipid droplets. The fatty acid composition was affected by the nature of the acyltransferase expressed. DGAT2 preferentially incorporated C16:1 fatty acids whereas DGAT1 displayed preference for C16:0, strongly suggesting that these enzymes have contrasting substrate specificities.Laure AyméSébastien BaudBertrand DubreucqFlorent JoffreThierry ChardotPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 3, p e92237 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Laure Aymé Sébastien Baud Bertrand Dubreucq Florent Joffre Thierry Chardot Function and localization of the Arabidopsis thaliana diacylglycerol acyltransferase DGAT2 expressed in yeast.
description	Diacylglycerol acyltransferases (DGATs) catalyze the final and only committed step of triacylglycerol synthesis. DGAT activity is rate limiting for triacylglycerol accumulation in mammals, plants and microbes. DGATs belong to three different evolutionary classes. In Arabidopsis thaliana, DGAT1, encoded by At2g19450, is the major DGAT enzyme involved in triacylglycerol accumulation in seeds. Until recently, the function of DGAT2 (At3g51520) has remained elusive. Previous attempts to characterize its enzymatic function by heterologous expression in yeast were unsuccessful. In the present report we demonstrate that expression of a codon-optimized version of the DGAT2 gene is able to restore neutral lipid accumulation in the Saccharomyces cerevisiae mutant strain (H1246), which is defective in triacylglycerol biosynthesis. Heterologous expression of codon-optimized DGAT2 and DGAT1 induced the biogenesis of subcellular lipid droplets containing triacylglycerols and squalene. Both DGAT proteins were found to be associated with these lipid droplets. The fatty acid composition was affected by the nature of the acyltransferase expressed. DGAT2 preferentially incorporated C16:1 fatty acids whereas DGAT1 displayed preference for C16:0, strongly suggesting that these enzymes have contrasting substrate specificities.
format	article
author	Laure Aymé Sébastien Baud Bertrand Dubreucq Florent Joffre Thierry Chardot
author_facet	Laure Aymé Sébastien Baud Bertrand Dubreucq Florent Joffre Thierry Chardot
author_sort	Laure Aymé
title	Function and localization of the Arabidopsis thaliana diacylglycerol acyltransferase DGAT2 expressed in yeast.
title_short	Function and localization of the Arabidopsis thaliana diacylglycerol acyltransferase DGAT2 expressed in yeast.
title_full	Function and localization of the Arabidopsis thaliana diacylglycerol acyltransferase DGAT2 expressed in yeast.
title_fullStr	Function and localization of the Arabidopsis thaliana diacylglycerol acyltransferase DGAT2 expressed in yeast.
title_full_unstemmed	Function and localization of the Arabidopsis thaliana diacylglycerol acyltransferase DGAT2 expressed in yeast.
title_sort	function and localization of the arabidopsis thaliana diacylglycerol acyltransferase dgat2 expressed in yeast.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/619dba49b04f40ab9206eba54ea9078c
work_keys_str_mv	AT laureayme functionandlocalizationofthearabidopsisthalianadiacylglycerolacyltransferasedgat2expressedinyeast AT sebastienbaud functionandlocalizationofthearabidopsisthalianadiacylglycerolacyltransferasedgat2expressedinyeast AT bertranddubreucq functionandlocalizationofthearabidopsisthalianadiacylglycerolacyltransferasedgat2expressedinyeast AT florentjoffre functionandlocalizationofthearabidopsisthalianadiacylglycerolacyltransferasedgat2expressedinyeast AT thierrychardot functionandlocalizationofthearabidopsisthalianadiacylglycerolacyltransferasedgat2expressedinyeast
_version_	1718421804543901696

Function and localization of the Arabidopsis thaliana diacylglycerol acyltransferase DGAT2 expressed in yeast.

Ejemplares similares