Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase
- Autores
- Iglesias, Alberto Alvaro; Ballicora, Miguel A.; Sesma, Juliana; Preiss, Jack
- Año de publicación
- 2006
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- ADP-glucose pyrophosphorylase (ADP-Glc PPase) catalyzes the regulatory step in the pathway for synthesis of bacterial glycogen and starch in plants. ADP-Glc PPases from cyanobacteria (homotetramer) and from potato (Solanum tuberosum) tuber (heterotetramer) are activated by 3-phosphoglycerate and inhibited by inorganic orthophosphate. To study the function of two putative domains, chimeric enzymes were constructed. PSSANA contained the N-terminus (292 amino acids) of the potato tuber ADP-Glc PPase small subunit (PSS) and the C-terminus (159 residues) of the Anabaena PCC 7120 enzyme. ANAPSS was the inverse chimera. These constructs were expressed separately or together with the large subunit of the potato tuber ADP-Glc PPase (PLS), to obtain homo- and heterotetrameric chimeric proteins. Characterization of these forms showed that the N-terminus determines stability and regulatory redox-dependent properties. The chimeric forms exhibited intermediate 3-phosphoglycerate activation properties with respect to the wild-type homotetrameric enzymes, indicating that the interaction between the putative N- and C-domains determines the affinity for the activator. Characterization of the chimeric heterotetramers showed the functionality of the large subunit, mainly in modulating regulation of the enzyme by the coordinate action of 3-phosphoglycerate and inorganic orthophosphate.
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Ballicora, Miguel A.. Loyola University Of Chicago;
Fil: Sesma, Juliana. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina
Fil: Preiss, Jack. Michigan State University; Estados Unidos - Materia
-
ADP-GLUCOSE PYROPHOSPHORYLASE
CYANOBACTERIA
GLYCOGEN SYNTHESIS
METABOLIC REGULATION
POTATO TUBER
STARCH SYNTHESIS - 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:11336/85781
Ver los metadatos del registro completo
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Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylaseIglesias, Alberto AlvaroBallicora, Miguel A.Sesma, JulianaPreiss, JackADP-GLUCOSE PYROPHOSPHORYLASECYANOBACTERIAGLYCOGEN SYNTHESISMETABOLIC REGULATIONPOTATO TUBERSTARCH SYNTHESIShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1ADP-glucose pyrophosphorylase (ADP-Glc PPase) catalyzes the regulatory step in the pathway for synthesis of bacterial glycogen and starch in plants. ADP-Glc PPases from cyanobacteria (homotetramer) and from potato (Solanum tuberosum) tuber (heterotetramer) are activated by 3-phosphoglycerate and inhibited by inorganic orthophosphate. To study the function of two putative domains, chimeric enzymes were constructed. PSSANA contained the N-terminus (292 amino acids) of the potato tuber ADP-Glc PPase small subunit (PSS) and the C-terminus (159 residues) of the Anabaena PCC 7120 enzyme. ANAPSS was the inverse chimera. These constructs were expressed separately or together with the large subunit of the potato tuber ADP-Glc PPase (PLS), to obtain homo- and heterotetrameric chimeric proteins. Characterization of these forms showed that the N-terminus determines stability and regulatory redox-dependent properties. The chimeric forms exhibited intermediate 3-phosphoglycerate activation properties with respect to the wild-type homotetrameric enzymes, indicating that the interaction between the putative N- and C-domains determines the affinity for the activator. Characterization of the chimeric heterotetramers showed the functionality of the large subunit, mainly in modulating regulation of the enzyme by the coordinate action of 3-phosphoglycerate and inorganic orthophosphate.Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; ArgentinaFil: Ballicora, Miguel A.. Loyola University Of Chicago;Fil: Sesma, Juliana. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFil: Preiss, Jack. Michigan State University; Estados UnidosOxford University Press2006-02info: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/11336/85781Iglesias, Alberto Alvaro; Ballicora, Miguel A.; Sesma, Juliana; Preiss, Jack; Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase; Oxford University Press; Plant And Cell Physiology; 47; 4; 2-2006; 523-5300032-0781CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.ncbi.nlm.nih.gov/pubmed/?term=Domain+swapping+between+a+cyanobaterial+and+a+plant+subunit+ADP-glucose+pyrophosphorylaseinfo:eu-repo/semantics/altIdentifier/doi/10.1093/pcp/pcj021info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:17:17Zoai:ri.conicet.gov.ar:11336/85781instacron: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:34982025-09-29 10:17:18.115CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase |
title |
Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase |
spellingShingle |
Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase Iglesias, Alberto Alvaro ADP-GLUCOSE PYROPHOSPHORYLASE CYANOBACTERIA GLYCOGEN SYNTHESIS METABOLIC REGULATION POTATO TUBER STARCH SYNTHESIS |
title_short |
Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase |
title_full |
Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase |
title_fullStr |
Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase |
title_full_unstemmed |
Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase |
title_sort |
Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase |
dc.creator.none.fl_str_mv |
Iglesias, Alberto Alvaro Ballicora, Miguel A. Sesma, Juliana Preiss, Jack |
author |
Iglesias, Alberto Alvaro |
author_facet |
Iglesias, Alberto Alvaro Ballicora, Miguel A. Sesma, Juliana Preiss, Jack |
author_role |
author |
author2 |
Ballicora, Miguel A. Sesma, Juliana Preiss, Jack |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
ADP-GLUCOSE PYROPHOSPHORYLASE CYANOBACTERIA GLYCOGEN SYNTHESIS METABOLIC REGULATION POTATO TUBER STARCH SYNTHESIS |
topic |
ADP-GLUCOSE PYROPHOSPHORYLASE CYANOBACTERIA GLYCOGEN SYNTHESIS METABOLIC REGULATION POTATO TUBER STARCH SYNTHESIS |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
ADP-glucose pyrophosphorylase (ADP-Glc PPase) catalyzes the regulatory step in the pathway for synthesis of bacterial glycogen and starch in plants. ADP-Glc PPases from cyanobacteria (homotetramer) and from potato (Solanum tuberosum) tuber (heterotetramer) are activated by 3-phosphoglycerate and inhibited by inorganic orthophosphate. To study the function of two putative domains, chimeric enzymes were constructed. PSSANA contained the N-terminus (292 amino acids) of the potato tuber ADP-Glc PPase small subunit (PSS) and the C-terminus (159 residues) of the Anabaena PCC 7120 enzyme. ANAPSS was the inverse chimera. These constructs were expressed separately or together with the large subunit of the potato tuber ADP-Glc PPase (PLS), to obtain homo- and heterotetrameric chimeric proteins. Characterization of these forms showed that the N-terminus determines stability and regulatory redox-dependent properties. The chimeric forms exhibited intermediate 3-phosphoglycerate activation properties with respect to the wild-type homotetrameric enzymes, indicating that the interaction between the putative N- and C-domains determines the affinity for the activator. Characterization of the chimeric heterotetramers showed the functionality of the large subunit, mainly in modulating regulation of the enzyme by the coordinate action of 3-phosphoglycerate and inorganic orthophosphate. Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina Fil: Ballicora, Miguel A.. Loyola University Of Chicago; Fil: Sesma, Juliana. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina Fil: Preiss, Jack. Michigan State University; Estados Unidos |
description |
ADP-glucose pyrophosphorylase (ADP-Glc PPase) catalyzes the regulatory step in the pathway for synthesis of bacterial glycogen and starch in plants. ADP-Glc PPases from cyanobacteria (homotetramer) and from potato (Solanum tuberosum) tuber (heterotetramer) are activated by 3-phosphoglycerate and inhibited by inorganic orthophosphate. To study the function of two putative domains, chimeric enzymes were constructed. PSSANA contained the N-terminus (292 amino acids) of the potato tuber ADP-Glc PPase small subunit (PSS) and the C-terminus (159 residues) of the Anabaena PCC 7120 enzyme. ANAPSS was the inverse chimera. These constructs were expressed separately or together with the large subunit of the potato tuber ADP-Glc PPase (PLS), to obtain homo- and heterotetrameric chimeric proteins. Characterization of these forms showed that the N-terminus determines stability and regulatory redox-dependent properties. The chimeric forms exhibited intermediate 3-phosphoglycerate activation properties with respect to the wild-type homotetrameric enzymes, indicating that the interaction between the putative N- and C-domains determines the affinity for the activator. Characterization of the chimeric heterotetramers showed the functionality of the large subunit, mainly in modulating regulation of the enzyme by the coordinate action of 3-phosphoglycerate and inorganic orthophosphate. |
publishDate |
2006 |
dc.date.none.fl_str_mv |
2006-02 |
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/11336/85781 Iglesias, Alberto Alvaro; Ballicora, Miguel A.; Sesma, Juliana; Preiss, Jack; Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase; Oxford University Press; Plant And Cell Physiology; 47; 4; 2-2006; 523-530 0032-0781 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/85781 |
identifier_str_mv |
Iglesias, Alberto Alvaro; Ballicora, Miguel A.; Sesma, Juliana; Preiss, Jack; Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase; Oxford University Press; Plant And Cell Physiology; 47; 4; 2-2006; 523-530 0032-0781 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://www.ncbi.nlm.nih.gov/pubmed/?term=Domain+swapping+between+a+cyanobaterial+and+a+plant+subunit+ADP-glucose+pyrophosphorylase info:eu-repo/semantics/altIdentifier/doi/10.1093/pcp/pcj021 |
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 |
Oxford University Press |
publisher.none.fl_str_mv |
Oxford University Press |
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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1844614124670025728 |
score |
13.070432 |