Tomato UDP-glucose sterol glycosyltransferases: A family of developmental and stress regulated genes that encode cytosolic and membrane-associated forms of the enzyme

Sterol glycosyltransferases (SGTs) catalyze the glycosylation of the free hydroxyl group at C-3 position of sterols to produce sterol glycosides. Glycosylated sterols and free sterols are primarily located in cell membranes where in combination with other membrane-bound lipids play a key role in mod...

Full description

Bibliographic Details
Authors: Ramírez Estrada, Karla; Castillo, Nídia; Lara, Juan A.; Arró i Plans, Montserrat; Boronat i Margosa, Albert; Ferrer i Prats, Albert; Altabella Artigas, Teresa
Format: Article
Status:Published version
Publication date:2017
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:2445/114783
Online Access:https://hdl.handle.net/2445/114783
Access Level:Open access
Keyword:Tomàquets
Arabidopsis
Glucòsids
Enzims
Tomatoes
Glucosides
Enzymes
_version_ 1878732225203142656
author Ramírez Estrada, Karla
author2 Castillo, Nídia
Lara, Juan A.
Arró i Plans, Montserrat
Boronat i Margosa, Albert
Ferrer i Prats, Albert
Altabella Artigas, Teresa
author2_role author
author
author
author
author
author
author_browse Altabella Artigas, Teresa
Arró i Plans, Montserrat
Boronat i Margosa, Albert
Castillo, Nídia
Ferrer i Prats, Albert
Lara, Juan A.
Ramírez Estrada, Karla
author_facet Ramírez Estrada, Karla
Castillo, Nídia
Lara, Juan A.
Arró i Plans, Montserrat
Boronat i Margosa, Albert
Ferrer i Prats, Albert
Altabella Artigas, Teresa
author_role author
collection Recercat. Dipósit de la Recerca de Catalunya
description Sterol glycosyltransferases (SGTs) catalyze the glycosylation of the free hydroxyl group at C-3 position of sterols to produce sterol glycosides. Glycosylated sterols and free sterols are primarily located in cell membranes where in combination with other membrane-bound lipids play a key role in modulating their properties and functioning. In contrast to most plant species, those of the genus Solanum contain very high levels of glycosylated sterols, which in the case of tomato may account for more than 85% of the total sterol content. In this study, we report the identification and functional characterization of the four members of the tomato (Solanum lycopersicum cv. Micro-Tom) SGT gene family. Expression of recombinant SlSGT proteins in E. coli cells and N. benthamiana leaves demonstrated the ability of the four enzymes to glycosylate different sterol species including cholesterol, brassicasterol, campesterol, stigmasterol, and β-sitosterol, which is consistent with the occurrence in their primary structure of the putative steroid-binding domain found in steroid UDP-glucuronosyltransferases and the UDP-sugar binding domain characteristic for a superfamily of nucleoside diphosphosugar glycosyltransferases. Subcellular localization studies based on fluorescence recovery after photobleaching and cell fractionation analyses revealed that the four tomato SGTs, like the Arabidopsis SGTs UGT80A2 and UGT80B1, localize into the cytosol and the PM, although there are clear differences in their relative distribution between these two cell fractions. The SlSGT genes have specialized but still largely overlapping expression patterns in different organs of tomato plants and throughout the different stages of fruit development and ripening. Moreover, they are differentially regulated in response to biotic and abiotic stress conditions. SlSGT4 expression increases markedly in response to osmotic, salt, and cold stress, as well as upon treatment with abscisic acid and methyl jasmonate.
eu_rights_str_mv openAccess
format article
id ES_3eeacaeba4e464dbfe4ee7292b5ed052
institution 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)
network_acronym_str ES
network_name_str España
oai_identifier_str oai:recercat.cat:2445/114783
publishDate 2017
publishDateSort 2017
publisher Frontiers Media
publisherStr Frontiers Media
reponame_str Recercat. Dipósit de la Recerca de Catalunya
spelling Tomato UDP-glucose sterol glycosyltransferases: A family of developmental and stress regulated genes that encode cytosolic and membrane-associated forms of the enzyme Ramírez Estrada, Karla Castillo, Nídia Lara, Juan A. Arró i Plans, Montserrat Boronat i Margosa, Albert Ferrer i Prats, Albert Altabella Artigas, Teresa Tomàquets Arabidopsis Glucòsids Enzims Tomatoes Glucosides Enzymes Sterol glycosyltransferases (SGTs) catalyze the glycosylation of the free hydroxyl group at C-3 position of sterols to produce sterol glycosides. Glycosylated sterols and free sterols are primarily located in cell membranes where in combination with other membrane-bound lipids play a key role in modulating their properties and functioning. In contrast to most plant species, those of the genus Solanum contain very high levels of glycosylated sterols, which in the case of tomato may account for more than 85% of the total sterol content. In this study, we report the identification and functional characterization of the four members of the tomato (Solanum lycopersicum cv. Micro-Tom) SGT gene family. Expression of recombinant SlSGT proteins in E. coli cells and N. benthamiana leaves demonstrated the ability of the four enzymes to glycosylate different sterol species including cholesterol, brassicasterol, campesterol, stigmasterol, and β-sitosterol, which is consistent with the occurrence in their primary structure of the putative steroid-binding domain found in steroid UDP-glucuronosyltransferases and the UDP-sugar binding domain characteristic for a superfamily of nucleoside diphosphosugar glycosyltransferases. Subcellular localization studies based on fluorescence recovery after photobleaching and cell fractionation analyses revealed that the four tomato SGTs, like the Arabidopsis SGTs UGT80A2 and UGT80B1, localize into the cytosol and the PM, although there are clear differences in their relative distribution between these two cell fractions. The SlSGT genes have specialized but still largely overlapping expression patterns in different organs of tomato plants and throughout the different stages of fruit development and ripening. Moreover, they are differentially regulated in response to biotic and abiotic stress conditions. SlSGT4 expression increases markedly in response to osmotic, salt, and cold stress, as well as upon treatment with abscisic acid and methyl jasmonate. Frontiers Media https://hdl.handle.net/2445/114783
spellingShingle Tomato UDP-glucose sterol glycosyltransferases: A family of developmental and stress regulated genes that encode cytosolic and membrane-associated forms of the enzyme
Ramírez Estrada, Karla
Tomàquets
Arabidopsis
Glucòsids
Enzims
Tomatoes
Glucosides
Enzymes
status_str publishedVersion
title Tomato UDP-glucose sterol glycosyltransferases: A family of developmental and stress regulated genes that encode cytosolic and membrane-associated forms of the enzyme
title_full Tomato UDP-glucose sterol glycosyltransferases: A family of developmental and stress regulated genes that encode cytosolic and membrane-associated forms of the enzyme
title_fullStr Tomato UDP-glucose sterol glycosyltransferases: A family of developmental and stress regulated genes that encode cytosolic and membrane-associated forms of the enzyme
title_full_unstemmed Tomato UDP-glucose sterol glycosyltransferases: A family of developmental and stress regulated genes that encode cytosolic and membrane-associated forms of the enzyme
title_short Tomato UDP-glucose sterol glycosyltransferases: A family of developmental and stress regulated genes that encode cytosolic and membrane-associated forms of the enzyme
title_sort Tomato UDP-glucose sterol glycosyltransferases: A family of developmental and stress regulated genes that encode cytosolic and membrane-associated forms of the enzyme
topic Tomàquets
Arabidopsis
Glucòsids
Enzims
Tomatoes
Glucosides
Enzymes
topic_facet Tomàquets
Arabidopsis
Glucòsids
Enzims
Tomatoes
Glucosides
Enzymes
url https://hdl.handle.net/2445/114783