Identification of a Bifunctional Maize C- and O-Glucosyltransferase

Autores
Falcone Ferreyra, María Lorena; Rodriguez, Eduardo Jose; Casas, María Isabel; Labadie, Guillermo Roberto; Grotewold, Erich; Casati, Paula
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Flavonoids accumulate in plant vacuoles usually as O-glycosylated derivatives, but several species can also synthesize flavonoid C-glycosides. Recently, we demonstrated that a flavanone 2-hydroxylase (ZmF2H1, CYP93G5) converts flavanones to the corresponding 2-hydroxy derivatives, which are expected to serve as substrates for C-glycosylation. Here, we isolated a cDNA encoding a UDP-dependent glycosyltransferase (UGT708A6), and its activity was characterized by in vitro and in vivo bioconversion assays. In vitro assays using 2-hydroxyflavanones as substrates and in vivo activity assays in yeast co-expressing ZmF2H1 and UGT708A6 show the formation of the flavones C-glycosides. UGT708A6 can also O-glycosylate flavanones in bioconversion assays in Escherichia coli as well as by in vitro assays with the purified recombinant protein. Thus, UGT708A6 is a bifunctional glycosyltransferase that can produce both C- and O-glycosidated flavonoids, a property not previously described for any other glycosyltransferase.
Fil: Falcone Ferreyra, María Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Fil: Rodriguez, Eduardo Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Casas, María Isabel. The Ohio State University. Plant Biotechnology Center. Department Plant Cell Molecular Biology; Estados Unidos
Fil: Labadie, Guillermo Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; Argentina
Fil: Grotewold, Erich. The Ohio State University. Plant Biotechnology Center; Estados Unidos
Fil: Casati, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Materia
Flavonoids
Glycosyltransferase
Maize
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/7832
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/7832
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Identification of a Bifunctional Maize C- and O-GlucosyltransferaseFalcone Ferreyra, María LorenaRodriguez, Eduardo JoseCasas, María IsabelLabadie, Guillermo RobertoGrotewold, ErichCasati, PaulaFlavonoidsGlycosyltransferaseMaizehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Flavonoids accumulate in plant vacuoles usually as O-glycosylated derivatives, but several species can also synthesize flavonoid C-glycosides. Recently, we demonstrated that a flavanone 2-hydroxylase (ZmF2H1, CYP93G5) converts flavanones to the corresponding 2-hydroxy derivatives, which are expected to serve as substrates for C-glycosylation. Here, we isolated a cDNA encoding a UDP-dependent glycosyltransferase (UGT708A6), and its activity was characterized by in vitro and in vivo bioconversion assays. In vitro assays using 2-hydroxyflavanones as substrates and in vivo activity assays in yeast co-expressing ZmF2H1 and UGT708A6 show the formation of the flavones C-glycosides. UGT708A6 can also O-glycosylate flavanones in bioconversion assays in Escherichia coli as well as by in vitro assays with the purified recombinant protein. Thus, UGT708A6 is a bifunctional glycosyltransferase that can produce both C- and O-glycosidated flavonoids, a property not previously described for any other glycosyltransferase.Fil: Falcone Ferreyra, María Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); ArgentinaFil: Rodriguez, Eduardo Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Casas, María Isabel. The Ohio State University. Plant Biotechnology Center. Department Plant Cell Molecular Biology; Estados UnidosFil: Labadie, Guillermo Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; ArgentinaFil: Grotewold, Erich. The Ohio State University. Plant Biotechnology Center; Estados UnidosFil: Casati, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); ArgentinaAmerican Society For Biochemistry And Molecular Biology2013-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/7832Falcone Ferreyra, María Lorena; Rodriguez, Eduardo Jose; Casas, María Isabel; Labadie, Guillermo Roberto; Grotewold, Erich; et al.; Identification of a Bifunctional Maize C- and O-Glucosyltransferase; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 288; 44; 10-2013; 31678-316880021-9258enginfo:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3814763/info:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/altIdentifier/url/http://dx.doi.org/10.1074/jbc.M113.510040info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:43:56Zoai:ri.conicet.gov.ar:11336/7832instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 14:43:56.431CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Identification of a Bifunctional Maize C- and O-Glucosyltransferase
title Identification of a Bifunctional Maize C- and O-Glucosyltransferase
spellingShingle Identification of a Bifunctional Maize C- and O-Glucosyltransferase
Falcone Ferreyra, María Lorena
Flavonoids
Glycosyltransferase
Maize
title_short Identification of a Bifunctional Maize C- and O-Glucosyltransferase
title_full Identification of a Bifunctional Maize C- and O-Glucosyltransferase
title_fullStr Identification of a Bifunctional Maize C- and O-Glucosyltransferase
title_full_unstemmed Identification of a Bifunctional Maize C- and O-Glucosyltransferase
title_sort Identification of a Bifunctional Maize C- and O-Glucosyltransferase
dc.creator.none.fl_str_mv Falcone Ferreyra, María Lorena
Rodriguez, Eduardo Jose
Casas, María Isabel
Labadie, Guillermo Roberto
Grotewold, Erich
Casati, Paula
author Falcone Ferreyra, María Lorena
author_facet Falcone Ferreyra, María Lorena
Rodriguez, Eduardo Jose
Casas, María Isabel
Labadie, Guillermo Roberto
Grotewold, Erich
Casati, Paula
author_role author
author2 Rodriguez, Eduardo Jose
Casas, María Isabel
Labadie, Guillermo Roberto
Grotewold, Erich
Casati, Paula
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Flavonoids
Glycosyltransferase
Maize
topic Flavonoids
Glycosyltransferase
Maize
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Flavonoids accumulate in plant vacuoles usually as O-glycosylated derivatives, but several species can also synthesize flavonoid C-glycosides. Recently, we demonstrated that a flavanone 2-hydroxylase (ZmF2H1, CYP93G5) converts flavanones to the corresponding 2-hydroxy derivatives, which are expected to serve as substrates for C-glycosylation. Here, we isolated a cDNA encoding a UDP-dependent glycosyltransferase (UGT708A6), and its activity was characterized by in vitro and in vivo bioconversion assays. In vitro assays using 2-hydroxyflavanones as substrates and in vivo activity assays in yeast co-expressing ZmF2H1 and UGT708A6 show the formation of the flavones C-glycosides. UGT708A6 can also O-glycosylate flavanones in bioconversion assays in Escherichia coli as well as by in vitro assays with the purified recombinant protein. Thus, UGT708A6 is a bifunctional glycosyltransferase that can produce both C- and O-glycosidated flavonoids, a property not previously described for any other glycosyltransferase.
Fil: Falcone Ferreyra, María Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Fil: Rodriguez, Eduardo Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Casas, María Isabel. The Ohio State University. Plant Biotechnology Center. Department Plant Cell Molecular Biology; Estados Unidos
Fil: Labadie, Guillermo Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; Argentina
Fil: Grotewold, Erich. The Ohio State University. Plant Biotechnology Center; Estados Unidos
Fil: Casati, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
description Flavonoids accumulate in plant vacuoles usually as O-glycosylated derivatives, but several species can also synthesize flavonoid C-glycosides. Recently, we demonstrated that a flavanone 2-hydroxylase (ZmF2H1, CYP93G5) converts flavanones to the corresponding 2-hydroxy derivatives, which are expected to serve as substrates for C-glycosylation. Here, we isolated a cDNA encoding a UDP-dependent glycosyltransferase (UGT708A6), and its activity was characterized by in vitro and in vivo bioconversion assays. In vitro assays using 2-hydroxyflavanones as substrates and in vivo activity assays in yeast co-expressing ZmF2H1 and UGT708A6 show the formation of the flavones C-glycosides. UGT708A6 can also O-glycosylate flavanones in bioconversion assays in Escherichia coli as well as by in vitro assays with the purified recombinant protein. Thus, UGT708A6 is a bifunctional glycosyltransferase that can produce both C- and O-glycosidated flavonoids, a property not previously described for any other glycosyltransferase.
publishDate 2013
dc.date.none.fl_str_mv 2013-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/7832
Falcone Ferreyra, María Lorena; Rodriguez, Eduardo Jose; Casas, María Isabel; Labadie, Guillermo Roberto; Grotewold, Erich; et al.; Identification of a Bifunctional Maize C- and O-Glucosyltransferase; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 288; 44; 10-2013; 31678-31688
0021-9258
url http://hdl.handle.net/11336/7832
identifier_str_mv Falcone Ferreyra, María Lorena; Rodriguez, Eduardo Jose; Casas, María Isabel; Labadie, Guillermo Roberto; Grotewold, Erich; et al.; Identification of a Bifunctional Maize C- and O-Glucosyltransferase; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 288; 44; 10-2013; 31678-31688
0021-9258
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3814763/
info:eu-repo/semantics/altIdentifier/doi/
info:eu-repo/semantics/altIdentifier/url/http://dx.doi.org/10.1074/jbc.M113.510040
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society For Biochemistry And Molecular Biology
publisher.none.fl_str_mv American Society For Biochemistry And Molecular Biology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.22299

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