A CDPK type protein kinase is involved in rice SPS light modulation
- Autores
- Pagnussat, Gabriela Carolina; Fiol, Diego Fernando; Salerno, Graciela Lidia
- Año de publicación
- 2002
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- A protein kinase activity that can phosphorylate and inactivate rice (Oryza sativa) sucrose-phosphate synthase (SPS; UDP-glucose: D-fructose-6-phosphate-2-glucosyl transferase, EC 2.4.1.14) was measured in extracts prepared from leaves exposed to light-dark transitions. Enzyme activity present in extracts from dark leaves was about 5-fold higher than the activity in extracts from leaves that had been collected in the light. The protein kinase (named R-SPSK) was purified about 100-fold from dark leaves and its biochemical properties were studied. The micromolar dependence of Ca2+ exhibited by R-SPSK, and its response to calmodulin antagonists was similar to the properties associated with members of the plant Calcium-Dependent Protein Kinase (CDPK) family. Two modulators of SPS activity, Pi and Glc-6-P, were examined for an effect on R-SPSK. While Glc-6-P did not affect R-SPSK activity, Pi drastically increased the kinase activity. Taken together, these data provide evidence that SPS may be regulated by a CDPK type protein-kinase whose activity is modulated by light-dark transitions and stimulated by Pi, the negative effector of SPS activity.
Fil: Pagnussat, Gabriela Carolina. Fundación para Investigaciones Biológicas Aplicadas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario; Argentina
Fil: Fiol, Diego Fernando. Fundación para Investigaciones Biológicas Aplicadas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario; Argentina
Fil: Salerno, Graciela Lidia. Fundación para Investigaciones Biológicas Aplicadas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario; Argentina - Materia
-
Sucrose
CDPK
Kinase
SPS - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/134578
Ver los metadatos del registro completo
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A CDPK type protein kinase is involved in rice SPS light modulationPagnussat, Gabriela CarolinaFiol, Diego FernandoSalerno, Graciela LidiaSucroseCDPKKinaseSPShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1A protein kinase activity that can phosphorylate and inactivate rice (Oryza sativa) sucrose-phosphate synthase (SPS; UDP-glucose: D-fructose-6-phosphate-2-glucosyl transferase, EC 2.4.1.14) was measured in extracts prepared from leaves exposed to light-dark transitions. Enzyme activity present in extracts from dark leaves was about 5-fold higher than the activity in extracts from leaves that had been collected in the light. The protein kinase (named R-SPSK) was purified about 100-fold from dark leaves and its biochemical properties were studied. The micromolar dependence of Ca2+ exhibited by R-SPSK, and its response to calmodulin antagonists was similar to the properties associated with members of the plant Calcium-Dependent Protein Kinase (CDPK) family. Two modulators of SPS activity, Pi and Glc-6-P, were examined for an effect on R-SPSK. While Glc-6-P did not affect R-SPSK activity, Pi drastically increased the kinase activity. Taken together, these data provide evidence that SPS may be regulated by a CDPK type protein-kinase whose activity is modulated by light-dark transitions and stimulated by Pi, the negative effector of SPS activity.Fil: Pagnussat, Gabriela Carolina. Fundación para Investigaciones Biológicas Aplicadas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario; ArgentinaFil: Fiol, Diego Fernando. Fundación para Investigaciones Biológicas Aplicadas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario; ArgentinaFil: Salerno, Graciela Lidia. Fundación para Investigaciones Biológicas Aplicadas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario; ArgentinaWiley Blackwell Publishing, Inc2002-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/134578Pagnussat, Gabriela Carolina; Fiol, Diego Fernando; Salerno, Graciela Lidia; A CDPK type protein kinase is involved in rice SPS light modulation; Wiley Blackwell Publishing, Inc; Physiologia Plantarum; 115; 2; 6-2002; 183-1890031-93171399-3054CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1034/j.1399-3054.2002.1150202.xinfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1034/j.1399-3054.2002.1150202.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 Técnicas2025-09-03T09:44:24Zoai:ri.conicet.gov.ar:11336/134578instacron: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 09:44:25.204CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
A CDPK type protein kinase is involved in rice SPS light modulation |
title |
A CDPK type protein kinase is involved in rice SPS light modulation |
spellingShingle |
A CDPK type protein kinase is involved in rice SPS light modulation Pagnussat, Gabriela Carolina Sucrose CDPK Kinase SPS |
title_short |
A CDPK type protein kinase is involved in rice SPS light modulation |
title_full |
A CDPK type protein kinase is involved in rice SPS light modulation |
title_fullStr |
A CDPK type protein kinase is involved in rice SPS light modulation |
title_full_unstemmed |
A CDPK type protein kinase is involved in rice SPS light modulation |
title_sort |
A CDPK type protein kinase is involved in rice SPS light modulation |
dc.creator.none.fl_str_mv |
Pagnussat, Gabriela Carolina Fiol, Diego Fernando Salerno, Graciela Lidia |
author |
Pagnussat, Gabriela Carolina |
author_facet |
Pagnussat, Gabriela Carolina Fiol, Diego Fernando Salerno, Graciela Lidia |
author_role |
author |
author2 |
Fiol, Diego Fernando Salerno, Graciela Lidia |
author2_role |
author author |
dc.subject.none.fl_str_mv |
Sucrose CDPK Kinase SPS |
topic |
Sucrose CDPK Kinase 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 |
A protein kinase activity that can phosphorylate and inactivate rice (Oryza sativa) sucrose-phosphate synthase (SPS; UDP-glucose: D-fructose-6-phosphate-2-glucosyl transferase, EC 2.4.1.14) was measured in extracts prepared from leaves exposed to light-dark transitions. Enzyme activity present in extracts from dark leaves was about 5-fold higher than the activity in extracts from leaves that had been collected in the light. The protein kinase (named R-SPSK) was purified about 100-fold from dark leaves and its biochemical properties were studied. The micromolar dependence of Ca2+ exhibited by R-SPSK, and its response to calmodulin antagonists was similar to the properties associated with members of the plant Calcium-Dependent Protein Kinase (CDPK) family. Two modulators of SPS activity, Pi and Glc-6-P, were examined for an effect on R-SPSK. While Glc-6-P did not affect R-SPSK activity, Pi drastically increased the kinase activity. Taken together, these data provide evidence that SPS may be regulated by a CDPK type protein-kinase whose activity is modulated by light-dark transitions and stimulated by Pi, the negative effector of SPS activity. Fil: Pagnussat, Gabriela Carolina. Fundación para Investigaciones Biológicas Aplicadas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario; Argentina Fil: Fiol, Diego Fernando. Fundación para Investigaciones Biológicas Aplicadas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario; Argentina Fil: Salerno, Graciela Lidia. Fundación para Investigaciones Biológicas Aplicadas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario; Argentina |
description |
A protein kinase activity that can phosphorylate and inactivate rice (Oryza sativa) sucrose-phosphate synthase (SPS; UDP-glucose: D-fructose-6-phosphate-2-glucosyl transferase, EC 2.4.1.14) was measured in extracts prepared from leaves exposed to light-dark transitions. Enzyme activity present in extracts from dark leaves was about 5-fold higher than the activity in extracts from leaves that had been collected in the light. The protein kinase (named R-SPSK) was purified about 100-fold from dark leaves and its biochemical properties were studied. The micromolar dependence of Ca2+ exhibited by R-SPSK, and its response to calmodulin antagonists was similar to the properties associated with members of the plant Calcium-Dependent Protein Kinase (CDPK) family. Two modulators of SPS activity, Pi and Glc-6-P, were examined for an effect on R-SPSK. While Glc-6-P did not affect R-SPSK activity, Pi drastically increased the kinase activity. Taken together, these data provide evidence that SPS may be regulated by a CDPK type protein-kinase whose activity is modulated by light-dark transitions and stimulated by Pi, the negative effector of SPS activity. |
publishDate |
2002 |
dc.date.none.fl_str_mv |
2002-06 |
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/11336/134578 Pagnussat, Gabriela Carolina; Fiol, Diego Fernando; Salerno, Graciela Lidia; A CDPK type protein kinase is involved in rice SPS light modulation; Wiley Blackwell Publishing, Inc; Physiologia Plantarum; 115; 2; 6-2002; 183-189 0031-9317 1399-3054 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/134578 |
identifier_str_mv |
Pagnussat, Gabriela Carolina; Fiol, Diego Fernando; Salerno, Graciela Lidia; A CDPK type protein kinase is involved in rice SPS light modulation; Wiley Blackwell Publishing, Inc; Physiologia Plantarum; 115; 2; 6-2002; 183-189 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/doi/10.1034/j.1399-3054.2002.1150202.x info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1034/j.1399-3054.2002.1150202.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 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 |
_version_ |
1842268665010978816 |
score |
13.13397 |