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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/1624
Ver los metadatos del registro completo
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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 |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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13.070432 |