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Peroxisomal Malate Dehydrogenase is not essential for photorespiration in Arabidopsis but its absence causes an increase in the stoichiometry of photorespiratory CO2 Release

dc.contributor.authorCousins, Asaph
dc.contributor.authorPracharoenwttana, Itsara
dc.contributor.authorZhou, Wenxu
dc.contributor.authorSmith, S
dc.contributor.authorBadger, Murray
dc.date.accessioned2015-12-10T22:55:08Z
dc.date.issued2008
dc.date.updated2016-02-24T11:52:19Z
dc.description.abstractPeroxisomes are important for recycling carbon and nitrogen that would otherwise be lost during photorespiration. The reduction of hydroxypyruvate to glycerate catalyzed by hydroxypyruvate reductase (HPR) in the peroxisomes is thought to be facilitated by the production of NADH by peroxisomal malate dehydrogenase (PMDH). PMDH, which is encoded by two genes in Arabidopsis (Arabidopsis thaliana), reduces NAD+ to NADH via the oxidation of malate supplied from the cytoplasm to oxaloacetate. A double mutant lacking the expression of both PMDH genes was viable in air and had rates of photosynthesis only slightly lower than in the wild type. This is in contrast to other photorespiratory mutants, which have severely reduced rates of photosynthesis and require high CO2 to grow. The pmdh mutant had a higher O 2-dependent CO2 compensation point than the wild type, implying that either Rubisco specificity had changed or that the rate of CO 2 released per Rubisco oxygenation was increased in the pmdh plants. Rates of gross O2 evolution and uptake were similar in the pmdh and wild-type plants, indicating that chloroplast linear electron transport and photorespiratory O2 uptake were similar between genotypes. The CO2 postillumination burst and the rate of CO2 released during photorespiration were both greater in the pmdh mutant compared with the wild type, suggesting that the ratio of photorespiratory CO2 release to Rubisco oxygenation was altered in the pmdh mutant. Without PMDH in the peroxisome, the CO2 released per Rubisco oxygenation reaction can be increased by over 50%. In summary, PMDH is essential for maintaining optimal rates of photorespiration in air; however, in its absence, significant rates of photorespiration are still possible, indicating that there are additional mechanisms for supplying reductant to the peroxisomal HPR reaction or that the HPR reaction is altogether circumvented.
dc.identifier.issn0032-0889
dc.identifier.urihttp://hdl.handle.net/1885/59966
dc.publisherAmerican Society of Plant Biologists
dc.sourcePlant Physiology
dc.subjectKeywords: Arabidopsis protein; carbon; carbon dioxide; malate dehydrogenase; PMDH1 protein, Arabidopsis; PMDH2 protein, Arabidopsis; ribulosebisphosphate carboxylase; analysis of variance; Arabidopsis; article; enzymology; genetics; genotype; growth, development an
dc.titlePeroxisomal Malate Dehydrogenase is not essential for photorespiration in Arabidopsis but its absence causes an increase in the stoichiometry of photorespiratory CO2 Release
dc.typeJournal article
local.bibliographicCitation.issue2
local.bibliographicCitation.lastpage795
local.bibliographicCitation.startpage786
local.contributor.affiliationCousins, Asaph, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationPracharoenwttana, Itsara, University of Western Australia
local.contributor.affiliationZhou, Wenxu, University of Western Australia
local.contributor.affiliationSmith, S, University of Western Australia
local.contributor.affiliationBadger, Murray, College of Medicine, Biology and Environment, ANU
local.contributor.authoruidCousins, Asaph, u4345411
local.contributor.authoruidBadger, Murray, u8002735
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor060705 - Plant Physiology
local.identifier.ariespublicationu9204316xPUB515
local.identifier.citationvolume148
local.identifier.doi10.1104/pp.108.122622
local.identifier.scopusID2-s2.0-57749103852
local.identifier.thomsonID000259810400010
local.type.statusPublished Version

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