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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/85781
Acceder
id CONICETDig_115562e1bb6c718a03c0ed89ff6f169a
oai_identifier_str oai:ri.conicet.gov.ar:11336/85781
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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 Técnicas2025-10-15T15:14:34Zoai: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:34982025-10-15 15:14:34.97CONICET 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
_version_ 1846083293089366016
score 13.22299

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