Unraveling the Activation Mechanism of the Potato Tuber ADP-glucose Pyrophosphorylase

Autores
Figueroa, Carlos Maria; Kuhn, Misty L.; Falaschetti, Christine A.; Solamen, Ligin; Olsen, Kenneth W.; Ballicora, Miguel A.; Iglesias, Alberto Alvaro
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
ADP-glucose pyrophosphorylase regulates the synthesis of glycogen in bacteria and of starch in plants. The enzyme from plants is mainly activated by 3-phosphoglycerate and is a heterotetramer comprising two small and two large subunits. Here, we found that two highly conserved residues are critical for triggering the activation of the potato tuber ADP-glucose pyrophosphorylase, as shown by site-directed mutagenesis. Mutations in the small subunit, which bears the catalytic function in this potato tuber form, had a more dramatic effect on disrupting the allosteric activation than those introduced in the large subunit, which is mainly modulatory. Our results strongly agree with a model where the modified residues are located in loops responsible for triggering the allosteric activation signal for this enzyme, and the sensitivity to this activation correlates with the dynamics of these loops. In addition, previous biochemical data indicates that the triggering mechanism is widespread in the enzyme family, even though the activator and the quaternary structure are not conserved.
Fil: Figueroa, Carlos Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
Fil: Kuhn, Misty L.. Loyola University. Dept. of Chemistry and Biochem.; Estados Unidos de América;
Fil: Falaschetti, Christine A.. Loyola University. Dept. of Chemistry and Biochem.; Estados Unidos de América;
Fil: Solamen, Ligin. Loyola University. Dept. of Chemistry and Biochem.; Estados Unidos de América;
Fil: Olsen, Kenneth W.. Loyola University. Dept. of Chemistry and Biochem.; Estados Unidos de América;
Fil: Ballicora, Miguel A.. Loyola University. Dept. of Chemistry and Biochem.; Estados Unidos de América;
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
Materia
Starch biosynthesis
ADP-glucose pyrophosphorylase
Allosteric activation
Signal propagation
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:11336/1624

id CONICETDig_8de35a2e0f502d5d037d8b71fc602def
oai_identifier_str oai:ri.conicet.gov.ar:11336/1624
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Unraveling the Activation Mechanism of the Potato Tuber ADP-glucose PyrophosphorylaseFigueroa, Carlos MariaKuhn, Misty L.Falaschetti, Christine A.Solamen, LiginOlsen, Kenneth W.Ballicora, Miguel A.Iglesias, Alberto AlvaroStarch biosynthesisADP-glucose pyrophosphorylaseAllosteric activationSignal propagationhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1ADP-glucose pyrophosphorylase regulates the synthesis of glycogen in bacteria and of starch in plants. The enzyme from plants is mainly activated by 3-phosphoglycerate and is a heterotetramer comprising two small and two large subunits. Here, we found that two highly conserved residues are critical for triggering the activation of the potato tuber ADP-glucose pyrophosphorylase, as shown by site-directed mutagenesis. Mutations in the small subunit, which bears the catalytic function in this potato tuber form, had a more dramatic effect on disrupting the allosteric activation than those introduced in the large subunit, which is mainly modulatory. Our results strongly agree with a model where the modified residues are located in loops responsible for triggering the allosteric activation signal for this enzyme, and the sensitivity to this activation correlates with the dynamics of these loops. In addition, previous biochemical data indicates that the triggering mechanism is widespread in the enzyme family, even though the activator and the quaternary structure are not conserved.Fil: Figueroa, Carlos Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;Fil: Kuhn, Misty L.. Loyola University. Dept. of Chemistry and Biochem.; Estados Unidos de América;Fil: Falaschetti, Christine A.. Loyola University. Dept. of Chemistry and Biochem.; Estados Unidos de América;Fil: Solamen, Ligin. Loyola University. Dept. of Chemistry and Biochem.; Estados Unidos de América;Fil: Olsen, Kenneth W.. Loyola University. Dept. of Chemistry and Biochem.; Estados Unidos de América;Fil: Ballicora, Miguel A.. Loyola University. Dept. of Chemistry and Biochem.; Estados Unidos de América;Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;Public Library Science2013-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/1624Figueroa, Carlos Maria; Kuhn, Misty L.; Falaschetti, Christine A.; Solamen, Ligin; Olsen, Kenneth W.; et al.; Unraveling the Activation Mechanism of the Potato Tuber ADP-glucose Pyrophosphorylase; Public Library Science; Plos One; 8; 6; 6-2013; 66824-668351932-6203enginfo:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0066824info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:17:11Zoai:ri.conicet.gov.ar:11336/1624instacron: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 10:17:12.269CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Unraveling the Activation Mechanism of the Potato Tuber ADP-glucose Pyrophosphorylase
title Unraveling the Activation Mechanism of the Potato Tuber ADP-glucose Pyrophosphorylase
spellingShingle Unraveling the Activation Mechanism of the Potato Tuber ADP-glucose Pyrophosphorylase
Figueroa, Carlos Maria
Starch biosynthesis
ADP-glucose pyrophosphorylase
Allosteric activation
Signal propagation
title_short Unraveling the Activation Mechanism of the Potato Tuber ADP-glucose Pyrophosphorylase
title_full Unraveling the Activation Mechanism of the Potato Tuber ADP-glucose Pyrophosphorylase
title_fullStr Unraveling the Activation Mechanism of the Potato Tuber ADP-glucose Pyrophosphorylase
title_full_unstemmed Unraveling the Activation Mechanism of the Potato Tuber ADP-glucose Pyrophosphorylase
title_sort Unraveling the Activation Mechanism of the Potato Tuber ADP-glucose Pyrophosphorylase
dc.creator.none.fl_str_mv Figueroa, Carlos Maria
Kuhn, Misty L.
Falaschetti, Christine A.
Solamen, Ligin
Olsen, Kenneth W.
Ballicora, Miguel A.
Iglesias, Alberto Alvaro
author Figueroa, Carlos Maria
author_facet Figueroa, Carlos Maria
Kuhn, Misty L.
Falaschetti, Christine A.
Solamen, Ligin
Olsen, Kenneth W.
Ballicora, Miguel A.
Iglesias, Alberto Alvaro
author_role author
author2 Kuhn, Misty L.
Falaschetti, Christine A.
Solamen, Ligin
Olsen, Kenneth W.
Ballicora, Miguel A.
Iglesias, Alberto Alvaro
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Starch biosynthesis
ADP-glucose pyrophosphorylase
Allosteric activation
Signal propagation
topic Starch biosynthesis
ADP-glucose pyrophosphorylase
Allosteric activation
Signal propagation
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 regulates the synthesis of glycogen in bacteria and of starch in plants. The enzyme from plants is mainly activated by 3-phosphoglycerate and is a heterotetramer comprising two small and two large subunits. Here, we found that two highly conserved residues are critical for triggering the activation of the potato tuber ADP-glucose pyrophosphorylase, as shown by site-directed mutagenesis. Mutations in the small subunit, which bears the catalytic function in this potato tuber form, had a more dramatic effect on disrupting the allosteric activation than those introduced in the large subunit, which is mainly modulatory. Our results strongly agree with a model where the modified residues are located in loops responsible for triggering the allosteric activation signal for this enzyme, and the sensitivity to this activation correlates with the dynamics of these loops. In addition, previous biochemical data indicates that the triggering mechanism is widespread in the enzyme family, even though the activator and the quaternary structure are not conserved.
Fil: Figueroa, Carlos Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
Fil: Kuhn, Misty L.. Loyola University. Dept. of Chemistry and Biochem.; Estados Unidos de América;
Fil: Falaschetti, Christine A.. Loyola University. Dept. of Chemistry and Biochem.; Estados Unidos de América;
Fil: Solamen, Ligin. Loyola University. Dept. of Chemistry and Biochem.; Estados Unidos de América;
Fil: Olsen, Kenneth W.. Loyola University. Dept. of Chemistry and Biochem.; Estados Unidos de América;
Fil: Ballicora, Miguel A.. Loyola University. Dept. of Chemistry and Biochem.; Estados Unidos de América;
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
description ADP-glucose pyrophosphorylase regulates the synthesis of glycogen in bacteria and of starch in plants. The enzyme from plants is mainly activated by 3-phosphoglycerate and is a heterotetramer comprising two small and two large subunits. Here, we found that two highly conserved residues are critical for triggering the activation of the potato tuber ADP-glucose pyrophosphorylase, as shown by site-directed mutagenesis. Mutations in the small subunit, which bears the catalytic function in this potato tuber form, had a more dramatic effect on disrupting the allosteric activation than those introduced in the large subunit, which is mainly modulatory. Our results strongly agree with a model where the modified residues are located in loops responsible for triggering the allosteric activation signal for this enzyme, and the sensitivity to this activation correlates with the dynamics of these loops. In addition, previous biochemical data indicates that the triggering mechanism is widespread in the enzyme family, even though the activator and the quaternary structure are not conserved.
publishDate 2013
dc.date.none.fl_str_mv 2013-06
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/11336/1624
Figueroa, Carlos Maria; Kuhn, Misty L.; Falaschetti, Christine A.; Solamen, Ligin; Olsen, Kenneth W.; et al.; Unraveling the Activation Mechanism of the Potato Tuber ADP-glucose Pyrophosphorylase; Public Library Science; Plos One; 8; 6; 6-2013; 66824-66835
1932-6203
url http://hdl.handle.net/11336/1624
identifier_str_mv Figueroa, Carlos Maria; Kuhn, Misty L.; Falaschetti, Christine A.; Solamen, Ligin; Olsen, Kenneth W.; et al.; Unraveling the Activation Mechanism of the Potato Tuber ADP-glucose Pyrophosphorylase; Public Library Science; Plos One; 8; 6; 6-2013; 66824-66835
1932-6203
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0066824
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
dc.publisher.none.fl_str_mv Public Library Science
publisher.none.fl_str_mv Public Library Science
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_ 1844614122904223744
score 13.070432