Rice sucrose-phosphate synthase: Identification of an isoform specific for heterotrophic tissues with distinct metabolite regulation from the mature leaf enzyme

Autores
Pagnussat, Gabriela Carolina; Curatti, Leonardo; Salerno, Graciela Lidia
Año de publicación
2000
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Immunohistological analyses for rice (Oryza sati7a) sucrose- to Pi which also strongly decreased enzyme activation by phosphate synthase (SPS, UDP-glucose D-fructose-6-phos- Glc-6-P. SPS-2 was highly activated by Glc-6-P and phate-2-glucosyltransferase, EC 2.4.1.14) show that the showed low sensitivity to Pi. In vitro alkaline phosphatase protein is differently localized in photosynthetic and etio- treatment suggested that SPS-1 could be regulated as leaf lated leaves. Very little is known about SPS regulation in SPS in darkness and that SPS-2 is present in a dephosphoheterotrophic tissues; therefore, we studied the biochemical rylated state or is not regulated by protein phosphorylation. properties of the enzyme from etiolated seedlings and em- The relative MM value (116 kDa) estimated for both SPS bryo. Two SPS forms (SPS-1 and SPS-2) were partially forms in SDS-PAGE is identical to the rice leaf SPS purified from etiolated seedlings. The effects of Glc-6-P (ac- polypeptide. Taken together, these data led us to conclude tivator) and Pi (inhibitor) on SPS activities allowed us to that SPS-2 is an enzyme form only present in non-photodifferentiate the two forms. SPS-1 showed high sensitivity synthetic tissues.
Fil: Pagnussat, Gabriela Carolina. Universidad Nacional de la Patagonia "San Juan Bosco". Instituto de Biociencias de la Patagonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Instituto de Biociencias de la Patagonia; Argentina. Fundación para Investigaciones Biológicas Aplicadas; Argentina
Fil: Curatti, Leonardo. Universidad Nacional de la Patagonia "San Juan Bosco". Instituto de Biociencias de la Patagonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Instituto de Biociencias de la Patagonia; Argentina. Fundación para Investigaciones Biológicas Aplicadas; Argentina
Fil: Salerno, Graciela Lidia. Universidad Nacional de la Patagonia "San Juan Bosco". Instituto de Biociencias de la Patagonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Instituto de Biociencias de la Patagonia; Argentina. Fundación para Investigaciones Biológicas Aplicadas; Argentina
Materia
Sucrose
SPS
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:11336/150661
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/150661
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Rice sucrose-phosphate synthase: Identification of an isoform specific for heterotrophic tissues with distinct metabolite regulation from the mature leaf enzymePagnussat, Gabriela CarolinaCuratti, LeonardoSalerno, Graciela LidiaSucroseSPShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Immunohistological analyses for rice (Oryza sati7a) sucrose- to Pi which also strongly decreased enzyme activation by phosphate synthase (SPS, UDP-glucose D-fructose-6-phos- Glc-6-P. SPS-2 was highly activated by Glc-6-P and phate-2-glucosyltransferase, EC 2.4.1.14) show that the showed low sensitivity to Pi. In vitro alkaline phosphatase protein is differently localized in photosynthetic and etio- treatment suggested that SPS-1 could be regulated as leaf lated leaves. Very little is known about SPS regulation in SPS in darkness and that SPS-2 is present in a dephosphoheterotrophic tissues; therefore, we studied the biochemical rylated state or is not regulated by protein phosphorylation. properties of the enzyme from etiolated seedlings and em- The relative MM value (116 kDa) estimated for both SPS bryo. Two SPS forms (SPS-1 and SPS-2) were partially forms in SDS-PAGE is identical to the rice leaf SPS purified from etiolated seedlings. The effects of Glc-6-P (ac- polypeptide. Taken together, these data led us to conclude tivator) and Pi (inhibitor) on SPS activities allowed us to that SPS-2 is an enzyme form only present in non-photodifferentiate the two forms. SPS-1 showed high sensitivity synthetic tissues.Fil: Pagnussat, Gabriela Carolina. Universidad Nacional de la Patagonia "San Juan Bosco". Instituto de Biociencias de la Patagonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Instituto de Biociencias de la Patagonia; Argentina. Fundación para Investigaciones Biológicas Aplicadas; ArgentinaFil: Curatti, Leonardo. Universidad Nacional de la Patagonia "San Juan Bosco". Instituto de Biociencias de la Patagonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Instituto de Biociencias de la Patagonia; Argentina. Fundación para Investigaciones Biológicas Aplicadas; ArgentinaFil: Salerno, Graciela Lidia. Universidad Nacional de la Patagonia "San Juan Bosco". Instituto de Biociencias de la Patagonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Instituto de Biociencias de la Patagonia; Argentina. Fundación para Investigaciones Biológicas Aplicadas; ArgentinaWiley Blackwell Publishing, Inc2000-04info: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/11336/150661Pagnussat, Gabriela Carolina; Curatti, Leonardo; Salerno, Graciela Lidia; Rice sucrose-phosphate synthase: Identification of an isoform specific for heterotrophic tissues with distinct metabolite regulation from the mature leaf enzyme; Wiley Blackwell Publishing, Inc; Physiologia Plantarum; 108; 4; 4-2000; 337-3440031-93171399-3054CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1034/j.1399-3054.2000.t01-1-100401.xinfo:eu-repo/semantics/altIdentifier/doi/10.1034/j.1399-3054.2000.t01-1-100401.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 Técnicas2025-09-03T10:09:29Zoai:ri.conicet.gov.ar:11336/150661instacron: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 10:09:29.414CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Rice sucrose-phosphate synthase: Identification of an isoform specific for heterotrophic tissues with distinct metabolite regulation from the mature leaf enzyme
title Rice sucrose-phosphate synthase: Identification of an isoform specific for heterotrophic tissues with distinct metabolite regulation from the mature leaf enzyme
spellingShingle Rice sucrose-phosphate synthase: Identification of an isoform specific for heterotrophic tissues with distinct metabolite regulation from the mature leaf enzyme
Pagnussat, Gabriela Carolina
Sucrose
SPS
title_short Rice sucrose-phosphate synthase: Identification of an isoform specific for heterotrophic tissues with distinct metabolite regulation from the mature leaf enzyme
title_full Rice sucrose-phosphate synthase: Identification of an isoform specific for heterotrophic tissues with distinct metabolite regulation from the mature leaf enzyme
title_fullStr Rice sucrose-phosphate synthase: Identification of an isoform specific for heterotrophic tissues with distinct metabolite regulation from the mature leaf enzyme
title_full_unstemmed Rice sucrose-phosphate synthase: Identification of an isoform specific for heterotrophic tissues with distinct metabolite regulation from the mature leaf enzyme
title_sort Rice sucrose-phosphate synthase: Identification of an isoform specific for heterotrophic tissues with distinct metabolite regulation from the mature leaf enzyme
dc.creator.none.fl_str_mv Pagnussat, Gabriela Carolina
Curatti, Leonardo
Salerno, Graciela Lidia
author Pagnussat, Gabriela Carolina
author_facet Pagnussat, Gabriela Carolina
Curatti, Leonardo
Salerno, Graciela Lidia
author_role author
author2 Curatti, Leonardo
Salerno, Graciela Lidia
author2_role author
author
dc.subject.none.fl_str_mv Sucrose
SPS
topic Sucrose
SPS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Immunohistological analyses for rice (Oryza sati7a) sucrose- to Pi which also strongly decreased enzyme activation by phosphate synthase (SPS, UDP-glucose D-fructose-6-phos- Glc-6-P. SPS-2 was highly activated by Glc-6-P and phate-2-glucosyltransferase, EC 2.4.1.14) show that the showed low sensitivity to Pi. In vitro alkaline phosphatase protein is differently localized in photosynthetic and etio- treatment suggested that SPS-1 could be regulated as leaf lated leaves. Very little is known about SPS regulation in SPS in darkness and that SPS-2 is present in a dephosphoheterotrophic tissues; therefore, we studied the biochemical rylated state or is not regulated by protein phosphorylation. properties of the enzyme from etiolated seedlings and em- The relative MM value (116 kDa) estimated for both SPS bryo. Two SPS forms (SPS-1 and SPS-2) were partially forms in SDS-PAGE is identical to the rice leaf SPS purified from etiolated seedlings. The effects of Glc-6-P (ac- polypeptide. Taken together, these data led us to conclude tivator) and Pi (inhibitor) on SPS activities allowed us to that SPS-2 is an enzyme form only present in non-photodifferentiate the two forms. SPS-1 showed high sensitivity synthetic tissues.
Fil: Pagnussat, Gabriela Carolina. Universidad Nacional de la Patagonia "San Juan Bosco". Instituto de Biociencias de la Patagonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Instituto de Biociencias de la Patagonia; Argentina. Fundación para Investigaciones Biológicas Aplicadas; Argentina
Fil: Curatti, Leonardo. Universidad Nacional de la Patagonia "San Juan Bosco". Instituto de Biociencias de la Patagonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Instituto de Biociencias de la Patagonia; Argentina. Fundación para Investigaciones Biológicas Aplicadas; Argentina
Fil: Salerno, Graciela Lidia. Universidad Nacional de la Patagonia "San Juan Bosco". Instituto de Biociencias de la Patagonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Instituto de Biociencias de la Patagonia; Argentina. Fundación para Investigaciones Biológicas Aplicadas; Argentina
description Immunohistological analyses for rice (Oryza sati7a) sucrose- to Pi which also strongly decreased enzyme activation by phosphate synthase (SPS, UDP-glucose D-fructose-6-phos- Glc-6-P. SPS-2 was highly activated by Glc-6-P and phate-2-glucosyltransferase, EC 2.4.1.14) show that the showed low sensitivity to Pi. In vitro alkaline phosphatase protein is differently localized in photosynthetic and etio- treatment suggested that SPS-1 could be regulated as leaf lated leaves. Very little is known about SPS regulation in SPS in darkness and that SPS-2 is present in a dephosphoheterotrophic tissues; therefore, we studied the biochemical rylated state or is not regulated by protein phosphorylation. properties of the enzyme from etiolated seedlings and em- The relative MM value (116 kDa) estimated for both SPS bryo. Two SPS forms (SPS-1 and SPS-2) were partially forms in SDS-PAGE is identical to the rice leaf SPS purified from etiolated seedlings. The effects of Glc-6-P (ac- polypeptide. Taken together, these data led us to conclude tivator) and Pi (inhibitor) on SPS activities allowed us to that SPS-2 is an enzyme form only present in non-photodifferentiate the two forms. SPS-1 showed high sensitivity synthetic tissues.
publishDate 2000
dc.date.none.fl_str_mv 2000-04
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/11336/150661
Pagnussat, Gabriela Carolina; Curatti, Leonardo; Salerno, Graciela Lidia; Rice sucrose-phosphate synthase: Identification of an isoform specific for heterotrophic tissues with distinct metabolite regulation from the mature leaf enzyme; Wiley Blackwell Publishing, Inc; Physiologia Plantarum; 108; 4; 4-2000; 337-344
0031-9317
1399-3054
CONICET Digital
CONICET
url http://hdl.handle.net/11336/150661
identifier_str_mv Pagnussat, Gabriela Carolina; Curatti, Leonardo; Salerno, Graciela Lidia; Rice sucrose-phosphate synthase: Identification of an isoform specific for heterotrophic tissues with distinct metabolite regulation from the mature leaf enzyme; Wiley Blackwell Publishing, Inc; Physiologia Plantarum; 108; 4; 4-2000; 337-344
0031-9317
1399-3054
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/10.1034/j.1399-3054.2000.t01-1-100401.x
info:eu-repo/semantics/altIdentifier/doi/10.1034/j.1399-3054.2000.t01-1-100401.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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