Trehalose synthesis in Euglena gracilis (Euglenophyceae) occurs through an enzyme complex

Autores
Fiol, Diego Fernando; Salerno, Graciela Lidia
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The aim of this study was to isolate and characterize a trehalose-synthesizing enzyme from Euglena gracilis Klebs. After purification by anion exchange chromatography, gel filtration, isoelectric focusing, and native electrophoresis, trehalose-6-phosphate synthase (TPS, EC 2.4.1.15) and trehalose-6-phosphate phosphatase (TPP, EC 3.1.3.12) activities could not be separated. Consequently, a TPS/TPP enzyme complex of about 250 kDa was suggested as responsible for trehalose synthesis in E. gracilis. The TPS activity was shown to be highly specific for glucose-6-P, and UDP-Glc was the preferred glucose donor, but GDP-Glc and CDP-Glc could also act as TPS substrates. The TPP activity was highly specific for trehalose-6-P. In vitro phosphorylation assays revealed rapid decreases in TPS and TPP activities. These changes corresponded to variations in the elution profile of gel filtration chromatography after the phosphorylation treatment. Taken together, these results suggest that the proposed TPS/TPP complex might be regulated through a protein phosphorylation/dephosphorylation-mediated mechanism that could affect the association state of the complex. Such a regulatory mechanism might lead to a rapid change in trehalose synthesis in response to variations in environmental conditions.
Fil: Fiol, Diego Fernando. Fundación para Investigaciones Biológicas Aplicadas; Argentina. University of California at Davis; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina
Fil: Salerno, Graciela Lidia. Fundación para Investigaciones Biológicas Aplicadas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina
Materia
EUGLENA GRACILIS
PROTEIN PHOSPHORYLATION
TREHALOSE BIOSYNTHESIS
TREHALOSE-PHOSPHATE PHOSPHATASE
TREHALOSE-PHOSPHATE SYNTHASE
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:11336/132690
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/132690
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Trehalose synthesis in Euglena gracilis (Euglenophyceae) occurs through an enzyme complexFiol, Diego FernandoSalerno, Graciela LidiaEUGLENA GRACILISPROTEIN PHOSPHORYLATIONTREHALOSE BIOSYNTHESISTREHALOSE-PHOSPHATE PHOSPHATASETREHALOSE-PHOSPHATE SYNTHASEhttps://purl.org/becyt/ford/4.5https://purl.org/becyt/ford/4The aim of this study was to isolate and characterize a trehalose-synthesizing enzyme from Euglena gracilis Klebs. After purification by anion exchange chromatography, gel filtration, isoelectric focusing, and native electrophoresis, trehalose-6-phosphate synthase (TPS, EC 2.4.1.15) and trehalose-6-phosphate phosphatase (TPP, EC 3.1.3.12) activities could not be separated. Consequently, a TPS/TPP enzyme complex of about 250 kDa was suggested as responsible for trehalose synthesis in E. gracilis. The TPS activity was shown to be highly specific for glucose-6-P, and UDP-Glc was the preferred glucose donor, but GDP-Glc and CDP-Glc could also act as TPS substrates. The TPP activity was highly specific for trehalose-6-P. In vitro phosphorylation assays revealed rapid decreases in TPS and TPP activities. These changes corresponded to variations in the elution profile of gel filtration chromatography after the phosphorylation treatment. Taken together, these results suggest that the proposed TPS/TPP complex might be regulated through a protein phosphorylation/dephosphorylation-mediated mechanism that could affect the association state of the complex. Such a regulatory mechanism might lead to a rapid change in trehalose synthesis in response to variations in environmental conditions.Fil: Fiol, Diego Fernando. Fundación para Investigaciones Biológicas Aplicadas; Argentina. University of California at Davis; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; ArgentinaFil: Salerno, Graciela Lidia. Fundación para Investigaciones Biológicas Aplicadas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; ArgentinaWiley Blackwell Publishing, Inc2005-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/132690Fiol, Diego Fernando; Salerno, Graciela Lidia; Trehalose synthesis in Euglena gracilis (Euglenophyceae) occurs through an enzyme complex; Wiley Blackwell Publishing, Inc; Journal Of Phycology; 41; 4; 8-2005; 812-8181529-88170022-3646CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/full/10.1111/j.1529-8817.2005.00098.xinfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1529-8817.2005.00098.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:06:58Zoai:ri.conicet.gov.ar:11336/132690instacron: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:34982025-09-03 10:06:58.925CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Trehalose synthesis in Euglena gracilis (Euglenophyceae) occurs through an enzyme complex
title Trehalose synthesis in Euglena gracilis (Euglenophyceae) occurs through an enzyme complex
spellingShingle Trehalose synthesis in Euglena gracilis (Euglenophyceae) occurs through an enzyme complex
Fiol, Diego Fernando
EUGLENA GRACILIS
PROTEIN PHOSPHORYLATION
TREHALOSE BIOSYNTHESIS
TREHALOSE-PHOSPHATE PHOSPHATASE
TREHALOSE-PHOSPHATE SYNTHASE
title_short Trehalose synthesis in Euglena gracilis (Euglenophyceae) occurs through an enzyme complex
title_full Trehalose synthesis in Euglena gracilis (Euglenophyceae) occurs through an enzyme complex
title_fullStr Trehalose synthesis in Euglena gracilis (Euglenophyceae) occurs through an enzyme complex
title_full_unstemmed Trehalose synthesis in Euglena gracilis (Euglenophyceae) occurs through an enzyme complex
title_sort Trehalose synthesis in Euglena gracilis (Euglenophyceae) occurs through an enzyme complex
dc.creator.none.fl_str_mv Fiol, Diego Fernando
Salerno, Graciela Lidia
author Fiol, Diego Fernando
author_facet Fiol, Diego Fernando
Salerno, Graciela Lidia
author_role author
author2 Salerno, Graciela Lidia
author2_role author
dc.subject.none.fl_str_mv EUGLENA GRACILIS
PROTEIN PHOSPHORYLATION
TREHALOSE BIOSYNTHESIS
TREHALOSE-PHOSPHATE PHOSPHATASE
TREHALOSE-PHOSPHATE SYNTHASE
topic EUGLENA GRACILIS
PROTEIN PHOSPHORYLATION
TREHALOSE BIOSYNTHESIS
TREHALOSE-PHOSPHATE PHOSPHATASE
TREHALOSE-PHOSPHATE SYNTHASE
purl_subject.fl_str_mv https://purl.org/becyt/ford/4.5
https://purl.org/becyt/ford/4
dc.description.none.fl_txt_mv The aim of this study was to isolate and characterize a trehalose-synthesizing enzyme from Euglena gracilis Klebs. After purification by anion exchange chromatography, gel filtration, isoelectric focusing, and native electrophoresis, trehalose-6-phosphate synthase (TPS, EC 2.4.1.15) and trehalose-6-phosphate phosphatase (TPP, EC 3.1.3.12) activities could not be separated. Consequently, a TPS/TPP enzyme complex of about 250 kDa was suggested as responsible for trehalose synthesis in E. gracilis. The TPS activity was shown to be highly specific for glucose-6-P, and UDP-Glc was the preferred glucose donor, but GDP-Glc and CDP-Glc could also act as TPS substrates. The TPP activity was highly specific for trehalose-6-P. In vitro phosphorylation assays revealed rapid decreases in TPS and TPP activities. These changes corresponded to variations in the elution profile of gel filtration chromatography after the phosphorylation treatment. Taken together, these results suggest that the proposed TPS/TPP complex might be regulated through a protein phosphorylation/dephosphorylation-mediated mechanism that could affect the association state of the complex. Such a regulatory mechanism might lead to a rapid change in trehalose synthesis in response to variations in environmental conditions.
Fil: Fiol, Diego Fernando. Fundación para Investigaciones Biológicas Aplicadas; Argentina. University of California at Davis; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina
Fil: Salerno, Graciela Lidia. Fundación para Investigaciones Biológicas Aplicadas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina
description The aim of this study was to isolate and characterize a trehalose-synthesizing enzyme from Euglena gracilis Klebs. After purification by anion exchange chromatography, gel filtration, isoelectric focusing, and native electrophoresis, trehalose-6-phosphate synthase (TPS, EC 2.4.1.15) and trehalose-6-phosphate phosphatase (TPP, EC 3.1.3.12) activities could not be separated. Consequently, a TPS/TPP enzyme complex of about 250 kDa was suggested as responsible for trehalose synthesis in E. gracilis. The TPS activity was shown to be highly specific for glucose-6-P, and UDP-Glc was the preferred glucose donor, but GDP-Glc and CDP-Glc could also act as TPS substrates. The TPP activity was highly specific for trehalose-6-P. In vitro phosphorylation assays revealed rapid decreases in TPS and TPP activities. These changes corresponded to variations in the elution profile of gel filtration chromatography after the phosphorylation treatment. Taken together, these results suggest that the proposed TPS/TPP complex might be regulated through a protein phosphorylation/dephosphorylation-mediated mechanism that could affect the association state of the complex. Such a regulatory mechanism might lead to a rapid change in trehalose synthesis in response to variations in environmental conditions.
publishDate 2005
dc.date.none.fl_str_mv 2005-08
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/11336/132690
Fiol, Diego Fernando; Salerno, Graciela Lidia; Trehalose synthesis in Euglena gracilis (Euglenophyceae) occurs through an enzyme complex; Wiley Blackwell Publishing, Inc; Journal Of Phycology; 41; 4; 8-2005; 812-818
1529-8817
0022-3646
CONICET Digital
CONICET
url http://hdl.handle.net/11336/132690
identifier_str_mv Fiol, Diego Fernando; Salerno, Graciela Lidia; Trehalose synthesis in Euglena gracilis (Euglenophyceae) occurs through an enzyme complex; Wiley Blackwell Publishing, Inc; Journal Of Phycology; 41; 4; 8-2005; 812-818
1529-8817
0022-3646
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/full/10.1111/j.1529-8817.2005.00098.x
info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1529-8817.2005.00098.x
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
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
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 13.13397

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