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dc.contributor.author Welchen, Elina
dc.contributor.author Schmitz, Jessica
dc.contributor.author Fuchs, Philippe
dc.contributor.author García, Lucila
dc.contributor.author Wagner, Stephan
dc.contributor.author Wienstroer, Judith
dc.contributor.author Schertl, Peter
dc.contributor.author Braun, Hans Peter
dc.contributor.author Schwarzländer, Marcus
dc.contributor.author Gonzalez, Daniel Hector
dc.contributor.author Maurino, Verónica G.
dc.date.available 2018-05-16T19:30:09Z
dc.date.issued 2016-10
dc.identifier.citation Welchen, Elina; Schmitz, Jessica; Fuchs, Philippe; García, Lucila; Wagner, Stephan; et al.; D-lactate dehydrogenase links methylglyoxal degradation and electron transport through cytochrome; American Society of Plant Biologist; Plant Physiology; 172; 2; 10-2016; 901-912
dc.identifier.issn 0032-0889
dc.identifier.uri http://hdl.handle.net/11336/45422
dc.description.abstract Glycolysis generates methylglyoxal (MGO) as an unavoidable, cytotoxic by-product in plant cells. MGO scavenging is performed by the glyoxalase system, which produces D-lactate as an end product. D-Lactate dehydrogenase (D-LDH) is encoded by a single gene in Arabidopsis (Arabidopsis thaliana; At5g06580). It catalyzes in vitro the oxidation of D-lactate to pyruvate using flavin adenine dinucleotide as a cofactor; knowledge of its function in the context of the plant cell remains sketchy. Blue native-polyacrylamide gel electrophoresis of mitochondrial extracts combined with in gel activity assays using different substrates and tandem mass spectrometry allowed us to definitely show that D-LDH acts specifically on D-lactate, is active as a dimer, and does not associate with respiratory supercomplexes of the inner mitochondrial membrane. The combined use of cytochrome c (CYTc) loss-of-function mutants and respiratory complex III inhibitors showed that CYTc acts as the in vivo electron acceptor of D-LDH. CYTc loss-of-function mutants, as well as the D-LDH mutants, were more sensitive to D-lactate and MGO, indicating that they function in the same pathway. In addition, overexpression of D-LDH and CYTc increased tolerance to D-lactate and MGO. Together with fine-localization of D-LDH, the functional interaction with CYTc in vivo strongly suggests that D-lactate oxidation takes place in the mitochondrial intermembrane space, delivering electrons to the respiratory chain through CYTc. These results provide a comprehensive picture of the organization and function of D-LDH in the plant cell and exemplify how the plant mitochondrial respiratory chain can act as a multifunctional electron sink for reductant from cytosolic pathways.
dc.format application/pdf
dc.language.iso eng
dc.publisher American Society of Plant Biologist
dc.rights info:eu-repo/semantics/restrictedAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject CITOCROMO C
dc.subject D-LACTATO
dc.subject.classification Otras Ciencias Biológicas
dc.subject.classification Ciencias Biológicas
dc.subject.classification CIENCIAS NATURALES Y EXACTAS
dc.title D-lactate dehydrogenase links methylglyoxal degradation and electron transport through cytochrome
dc.type info:eu-repo/semantics/article
dc.type info:ar-repo/semantics/artículo
dc.type info:eu-repo/semantics/publishedVersion
dc.date.updated 2018-05-11T21:17:06Z
dc.journal.volume 172
dc.journal.number 2
dc.journal.pagination 901-912
dc.journal.pais Estados Unidos
dc.journal.ciudad Rockville
dc.description.fil Fil: Welchen, Elina. 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
dc.description.fil Fil: Schmitz, Jessica. Heinrich-Heine-Universität; Alemania
dc.description.fil Fil: Fuchs, Philippe. Universitat Bonn; Alemania
dc.description.fil Fil: García, Lucila. 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
dc.description.fil Fil: Wagner, Stephan. Universitat Bonn; Alemania
dc.description.fil Fil: Wienstroer, Judith. Heinrich-Heine-Universität; Alemania
dc.description.fil Fil: Schertl, Peter. Leibniz Universität Hannover; Alemania
dc.description.fil Fil: Braun, Hans Peter. Leibniz Universität Hannover; Alemania
dc.description.fil Fil: Schwarzländer, Marcus. Universitat Bonn; Alemania
dc.description.fil Fil: Gonzalez, Daniel Hector. 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
dc.description.fil Fil: Maurino, Verónica G.. Heinrich-Heine-Universität; Alemania
dc.journal.title Plant Physiology
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1104/pp.16.01174
dc.conicet.fuente Elsevier


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info:eu-repo/semantics/restrictedAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)