Identification and characterization of sterol acyltransferases responsible for steryl ester biosynthesis in tomato

Steryl esters (SEs) serve as a storage pool of sterols that helps to maintain proper levels of free sterols (FSs) in cell membranes throughout plant growth and development, and participates in the recycling of FSs and fatty acids released from cell membranes in aging tissues. SEs are synthesized by...

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Authors: Lara, Juan A., Burciaga Monge, Alma Delia, Chávez, Ángel, Revés, Marc, Lavilla Grífols, Rodolfo, Arró i Plans, Montserrat, Boronat i Margosa, Albert, Altabella Artigas, Teresa, Ferrer i Prats, Albert
Format: article
Status:Published version
Publication Date:2018
Country:España
Institution:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repository:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/122293
Online Access:https://hdl.handle.net/2445/122293
Access Level:Open access
Keyword:Arabidopsis
Biosíntesi
Tomàquets
Biosynthesis
Tomatoes
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spelling Identification and characterization of sterol acyltransferases responsible for steryl ester biosynthesis in tomatoLara, Juan A.Burciaga Monge, Alma DeliaChávez, ÁngelRevés, MarcLavilla Grífols, RodolfoArró i Plans, MontserratBoronat i Margosa, AlbertAltabella Artigas, TeresaFerrer i Prats, AlbertArabidopsisBiosíntesiTomàquetsArabidopsisBiosynthesisTomatoesSteryl esters (SEs) serve as a storage pool of sterols that helps to maintain proper levels of free sterols (FSs) in cell membranes throughout plant growth and development, and participates in the recycling of FSs and fatty acids released from cell membranes in aging tissues. SEs are synthesized by sterol acyltransferases, a family of enzymes that catalyze the transfer of fatty acil groups to the hydroxyl group at C-3 position of the sterol backbone. Sterol acyltransferases are categorized into acyl-CoA:sterol acyltransferases (ASAT) and phospholipid:sterol acyltransferases (PSAT) depending on whether the fatty acyl donor substrate is a long-chain acyl-CoA or a phospolipid. Until now, only Arabidopsis ASAT and PSAT enzymes (AtASAT1 and AtPSAT1) have been cloned and characterized in plants. Here we report the identification, cloning, and functional characterization of the tomato (Solanum lycopersicum cv. Micro-Tom) orthologs. SlPSAT1 and SlASAT1 were able to restore SE to wild type levels in the Arabidopsis psat1-2 and asat1-1 knock-out mutants, respectively. Expression of SlPSAT1 in the psat1-2 background also prevented the toxicity caused by an external supply of mevalonate and the early senescence phenotype observed in detached leaves of this mutant, whereas expression of SlASAT1 in the asat1-1 mutant revealed a clear substrate preference of the tomato enzyme for the sterol precursors cycloartenol and 24-methylene cycloartanol. Subcellular localization studies using fluorescently tagged SlPSAT1 and SlASAT1 proteins revealed that SlPSAT1 localize in cytoplasmic lipid droplets (LDs) while, in contrast to the endoplasmic reticulum (ER) localization of AtASAT1, SlASAT1 resides in the plasma membrane (PM). The possibility that PM-localized SlASAT1 may act catalytically in trans on their sterol substrates, which are presumably embedded in the ER membrane, is discussed. The widespread expression of SlPSAT1 and SlASAT1 genes in different tomato organs together with their moderate transcriptional response to several stresses suggests a dual role of SlPSAT1 and SlASAT1 in tomato plant and fruit development and the adaptive responses to stress. Overall, this study contributes to enlarge the current knowledge on plant sterol acyltransferases and set the basis for further studies aimed at understanding the role of SE metabolism in tomato plant growth and development.Frontiers Media2018201820182018info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion18 p.application/pdfhttps://hdl.handle.net/2445/122293Articles publicats en revistes (Bioquímica i Fisiologia)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: https://doi.org/10.3389/fpls.2018.00588Frontiers in Plant Science, 2018, vol. 9, num. 588https://doi.org/10.3389/fpls.2018.00588cc-by (c) Lara, Juan A. et al., 2018http://creativecommons.org/licenses/by/3.0/esinfo:eu-repo/semantics/openAccessoai:recercat.cat:2445/1222932026-05-29T05:05:01Z
dc.title.none.fl_str_mv Identification and characterization of sterol acyltransferases responsible for steryl ester biosynthesis in tomato
title Identification and characterization of sterol acyltransferases responsible for steryl ester biosynthesis in tomato
spellingShingle Identification and characterization of sterol acyltransferases responsible for steryl ester biosynthesis in tomato
Lara, Juan A.
Arabidopsis
Biosíntesi
Tomàquets
Arabidopsis
Biosynthesis
Tomatoes
title_short Identification and characterization of sterol acyltransferases responsible for steryl ester biosynthesis in tomato
title_full Identification and characterization of sterol acyltransferases responsible for steryl ester biosynthesis in tomato
title_fullStr Identification and characterization of sterol acyltransferases responsible for steryl ester biosynthesis in tomato
title_full_unstemmed Identification and characterization of sterol acyltransferases responsible for steryl ester biosynthesis in tomato
title_sort Identification and characterization of sterol acyltransferases responsible for steryl ester biosynthesis in tomato
dc.creator.none.fl_str_mv Lara, Juan A.
Burciaga Monge, Alma Delia
Chávez, Ángel
Revés, Marc
Lavilla Grífols, Rodolfo
Arró i Plans, Montserrat
Boronat i Margosa, Albert
Altabella Artigas, Teresa
Ferrer i Prats, Albert
author Lara, Juan A.
author_facet Lara, Juan A.
Burciaga Monge, Alma Delia
Chávez, Ángel
Revés, Marc
Lavilla Grífols, Rodolfo
Arró i Plans, Montserrat
Boronat i Margosa, Albert
Altabella Artigas, Teresa
Ferrer i Prats, Albert
author_role author
author2 Burciaga Monge, Alma Delia
Chávez, Ángel
Revés, Marc
Lavilla Grífols, Rodolfo
Arró i Plans, Montserrat
Boronat i Margosa, Albert
Altabella Artigas, Teresa
Ferrer i Prats, Albert
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Arabidopsis
Biosíntesi
Tomàquets
Arabidopsis
Biosynthesis
Tomatoes
topic Arabidopsis
Biosíntesi
Tomàquets
Arabidopsis
Biosynthesis
Tomatoes
description Steryl esters (SEs) serve as a storage pool of sterols that helps to maintain proper levels of free sterols (FSs) in cell membranes throughout plant growth and development, and participates in the recycling of FSs and fatty acids released from cell membranes in aging tissues. SEs are synthesized by sterol acyltransferases, a family of enzymes that catalyze the transfer of fatty acil groups to the hydroxyl group at C-3 position of the sterol backbone. Sterol acyltransferases are categorized into acyl-CoA:sterol acyltransferases (ASAT) and phospholipid:sterol acyltransferases (PSAT) depending on whether the fatty acyl donor substrate is a long-chain acyl-CoA or a phospolipid. Until now, only Arabidopsis ASAT and PSAT enzymes (AtASAT1 and AtPSAT1) have been cloned and characterized in plants. Here we report the identification, cloning, and functional characterization of the tomato (Solanum lycopersicum cv. Micro-Tom) orthologs. SlPSAT1 and SlASAT1 were able to restore SE to wild type levels in the Arabidopsis psat1-2 and asat1-1 knock-out mutants, respectively. Expression of SlPSAT1 in the psat1-2 background also prevented the toxicity caused by an external supply of mevalonate and the early senescence phenotype observed in detached leaves of this mutant, whereas expression of SlASAT1 in the asat1-1 mutant revealed a clear substrate preference of the tomato enzyme for the sterol precursors cycloartenol and 24-methylene cycloartanol. Subcellular localization studies using fluorescently tagged SlPSAT1 and SlASAT1 proteins revealed that SlPSAT1 localize in cytoplasmic lipid droplets (LDs) while, in contrast to the endoplasmic reticulum (ER) localization of AtASAT1, SlASAT1 resides in the plasma membrane (PM). The possibility that PM-localized SlASAT1 may act catalytically in trans on their sterol substrates, which are presumably embedded in the ER membrane, is discussed. The widespread expression of SlPSAT1 and SlASAT1 genes in different tomato organs together with their moderate transcriptional response to several stresses suggests a dual role of SlPSAT1 and SlASAT1 in tomato plant and fruit development and the adaptive responses to stress. Overall, this study contributes to enlarge the current knowledge on plant sterol acyltransferases and set the basis for further studies aimed at understanding the role of SE metabolism in tomato plant growth and development.
publishDate 2018
dc.date.none.fl_str_mv 2018
2018
2018
2018
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/122293
url https://hdl.handle.net/2445/122293
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.3389/fpls.2018.00588
Frontiers in Plant Science, 2018, vol. 9, num. 588
https://doi.org/10.3389/fpls.2018.00588
dc.rights.none.fl_str_mv cc-by (c) Lara, Juan A. et al., 2018
http://creativecommons.org/licenses/by/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) Lara, Juan A. et al., 2018
http://creativecommons.org/licenses/by/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 18 p.
application/pdf
dc.publisher.none.fl_str_mv Frontiers Media
publisher.none.fl_str_mv Frontiers Media
dc.source.none.fl_str_mv Articles publicats en revistes (Bioquímica i Fisiologia)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,81155

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