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dc.contributor.author
Kuhn, Misty
dc.contributor.author
Figueroa, Carlos Maria
dc.contributor.author
Iglesias, Alberto Alvaro
dc.contributor.author
Ballicora, Miguel A.
dc.date.available
2015-08-11T20:45:45Z
dc.date.issued
2013-02
dc.identifier.citation
Kuhn, Misty; Figueroa, Carlos Maria; Iglesias, Alberto Alvaro; Ballicora, Miguel A.; The Ancestral Activation Promiscuity of ADP-glucose Pyrophosphorylase from Photosynthetic Organisms; Biomed Central; Bmc Evolutionary Biology; 13; 2-2013; 51-60
dc.identifier.issn
1471-2148
dc.identifier.uri
http://hdl.handle.net/11336/1622
dc.description.abstract
ADP-glucose pyrophosphorylase (ADP-Glc PPase) catalyzes the first committed step in the synthesis of glycogen in bacteria and starch in algae and plants. In oxygenic photosynthetic organisms, ADP-Glc PPase is mainly activated by 3-phosphoglycerate (3-PGA) and to a lesser extent by other metabolites. In this work, we analyzed the activation promiscuity of ADP-Glc PPase subunits from the cyanobacterium Anabaena PCC 7120, the green alga Ostreococcus tauri, and potato (Solanum tuberosum) tuber by comparing a specificity constant for 3-PGA, fructose-1,6-bisphosphate (FBP), fructose-6-phosphate, and glucose-6-phosphate.The 3-PGA specificity constant for the enzymes from Anabaena (homotetramer), O. tauri, and potato tuber was considerably higher than for other activators. O. tauriand potato tuber enzymes were heterotetramers comprising homologous small and large subunits. Conversely, the O. tauri small subunit (OtaS) homotetramer was more promiscuous because its FBP specificity constant was similar to that for 3-PGA. To explore the role of both OtaS and OtaL ( O. tauri large subunit) in determining the specificity of the heterotetramer, we knocked out the catalytic activity of each subunit individually by site-directed mutagenesis. Interestingly, the mutants OtaS D148A /OtaL and OtaS/OtaL D171A had higher specificity constants for 3-PGA than for FBP. After gene duplication, OtaS seemed to have lost specificity for 3-PGA compared to FBP. This was physiologically and evolutionarily feasible because co-expression of both subunits restored the specificity for 3-PGA of the resulting heterotetrameric wild type enzyme. This widespread promiscuity seems to be ancestral and intrinsic to the enzyme family. Its presence could constitute an efficient evolutionary mechanism to accommodate the ADP-Glc PPase regulation to different metabolic needs.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Biomed Central
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Glycogen Synthesis
dc.subject
Allosteric Regulation
dc.subject
Evolutive Specificity
dc.subject
Photosynthesis
dc.subject.classification
Bioquímica y Biología Molecular
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
The Ancestral Activation Promiscuity of ADP-glucose Pyrophosphorylase from Photosynthetic Organisms
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-03-30 10:35:44.97925-03
dc.journal.volume
13
dc.journal.pagination
51-60
dc.journal.pais
Reino Unido
dc.journal.ciudad
Londres
dc.description.fil
Fil: Kuhn, Misty. Loyola University. Dept. Chem. & Biochem.; Estados Unidos de América;
dc.description.fil
Fil: Figueroa, Carlos Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
dc.description.fil
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
dc.description.fil
Fil: Ballicora, Miguel A.. Loyola University. Dept. Chem. & Biochem.; Estados Unidos de América;
dc.journal.title
Bmc Evolutionary Biology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.biomedcentral.com/1471-2148/13/51
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