<scp>d</scp>‐Lactate dehydrogenase as a marker gene allows positive selection of transgenic plants

Wienstroer, Judith; Engqvist, Martin K. M.; Kunz, Hans‐Henning; Flügge, Ulf‐Ingo; Maurino, Verónica G.

doi:10.1016/j.febslet.2011.11.020

Cited by 29 publications

(23 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Reduced GSH is released during this reaction. D-lactate is oxidized to pyruvate by the mitochondrial intermembrane space-localized D-lactate dehydrogenase (D-LDH), which passes the electrons to the electron transport chain via cytochrome c (CYTc) (Engqvist et al, 2009;Wienstroer et al, 2012;Welchen et al, 2016). Pyruvate finally enters the tricarboxylic acid cycle.…”

Section: Introductionmentioning

confidence: 99%

Defense against Reactive Carbonyl Species Involves at Least Three Subcellular Compartments Where Individual Components of the System Respond to Cellular Sugar Status

et al. 2017

Self Cite

View full text Add to dashboard Cite

Methylglyoxal (MGO) and glyoxal (GO) are toxic reactive carbonyl species generated as by-products of glycolysis. The pre-emption pathway for detoxification of these products, the glyoxalase (GLX) system, involves two consecutive reactions catalyzed by GLXI and GLXII. In , the GLX system is encoded by three homologs of and three homologs of , from which several predicted GLXI and GLXII isoforms can be derived through alternative splicing. We identified the physiologically relevant splice forms using sequencing data and demonstrated that the resulting isoforms have different subcellular localizations. All three GLXI homologs are functional in vivo, as they complemented a yeast GLXI loss-of-function mutant. Efficient MGO and GO detoxification can be controlled by a switch in metal cofactor usage. MGO formation is closely connected to the flux through glycolysis and through the Calvin Benson cycle; accordingly, expression analysis indicated that GLXI is transcriptionally regulated by endogenous sugar levels. Analyses of Arabidopsis loss-of-function lines revealed that the elimination of toxic reactive carbonyl species during germination and seedling establishment depends on the activity of the cytosolic GLXI;3 isoform. The Arabidopsis GLX system involves the cytosol, chloroplasts, and mitochondria, which harbor individual components that might be used at specific developmental stages and respond differentially to cellular sugar status.

show abstract

Section: Introductionmentioning

confidence: 99%

Defense against Reactive Carbonyl Species Involves at Least Three Subcellular Compartments Where Individual Components of the System Respond to Cellular Sugar Status

et al. 2017

Self Cite

View full text Add to dashboard Cite

show abstract

“…PtDH1 (UniProt ID B7GAH3) forms a strongly supported clade with sequences from the chlorophytes Chlamydomonas reinhardtii and Volvox carteri, streptophyta d-LDH (including the recently characterized A. thaliana d-LDH (Engqvist et al 2009;Welchen et al 2016;Wienstroer et al 2012)), animal d-LDH, and sequences from diverse bacteria.…”

Section: Diatoms Do Not Possess Orthologs Of Proteins With Known Glcdmentioning

confidence: 99%

“…Consistent with their usage of GOX, land plants, glaucophyta, rhodophyta, and charophyta do not possess GlcDH. They encode a homolog of cyanobacterial GlcDH, but this is not involved in glycolate metabolism but functions as a d-lactate dehydrogenase (d-LDH; EC 1.1.2.4) in mitochondria (Engqvist et al 2009;Welchen et al 2016;Wienstroer et al 2012).…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, the mutant strain excretes high amounts of glycolate and requires high CO 2 to survive. Diverse d-LDH homologs, including mitochondrial D-LDH of A. thaliana (Engqvist et al 2009;Welchen et al 2016;Wienstroer et al 2012), form a sister group to chlorophyte GlcDH and proteobacterial d-LDH (Nakamura et al 2005). Chlorophyta and cyanobacteria do not possess GOX.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The ancestors of diatoms evolved a unique mitochondrial dehydrogenase to oxidize photorespiratory glycolate

et al. 2017

Self Cite

View full text Add to dashboard Cite

Like other oxygenic photosynthetic organisms, diatoms produce glycolate, a toxic intermediate, as a consequence of the oxygenase activity of Rubisco. Diatoms can remove glycolate through excretion and through oxidation as part of the photorespiratory pathway. The diatom Phaeodactylum tricornutum encodes two proteins suggested to be involved in glycolate metabolism: PtGO1 and PtGO2. We found that these proteins differ substantially from the sequences of experimentally characterized proteins responsible for glycolate oxidation in other species, glycolate oxidase (GOX) and glycolate dehydrogenase. We show that PtGO1 and PtGO2 are the only sequences of P. tricornutum homologous to GOX. Our phylogenetic analyses indicate that the ancestors of diatoms acquired PtGO1 during the proposed first secondary endosymbiosis with a chlorophyte alga, which may have previously obtained this gene from proteobacteria. In contrast, PtGO2 is orthologous to an uncharacterized protein in Galdieria sulphuraria, consistent with its acquisition during the secondary endosymbiosis with a red alga that gave rise to the current plastid. The analysis of amino acid residues at conserved positions suggests that PtGO2, which localizes to peroxisomes, may use substrates other than glycolate, explaining the lack of GOX activity we observe in vitro. Instead, PtGO1, while only very distantly related to previously characterized GOX proteins, evolved glycolate-oxidizing activity, as demonstrated by in gel activity assays and mass spectrometry analysis. PtGO1 localizes to mitochondria, consistent with previous suggestions that photorespiration in diatoms proceeds in these organelles. We conclude that the ancestors of diatoms evolved a unique alternative to oxidize photorespiratory glycolate: a mitochondrial dehydrogenase homologous to GOX able to use electron acceptors other than O.

show abstract

“…In the second pathway, MGO also can be metabolized to D-lactate in a single step through the glutathione-independent cytosolic DJ-1d protein (EC 4.2.1.130;Kwon et al, 2013). This protein, a member of the PfpI/Hsp31/DJ-1 superfamily, can function as a hydrolyase that requires no cofactors (Misra et al, 1995;Subedi et al, 2011).In plants, D-lactate is metabolized by D-lactate dehydrogenase (D-LDH; At5g06580;Engqvist et al, 2009;Wienstroer et al, 2012). In addition to D-lactate, D-LDH also can use other compounds as substrates in vitro, such as L-lactate, glycolate, and D-glycerate.…”

mentioning

confidence: 99%

D-Lactate dehydrogenase links methylglyoxal degradation and electron transport through cytochrome C

et al. 2016

Self Cite

View full text Add to dashboard Cite

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.

show abstract

d‐Lactate dehydrogenase as a marker gene allows positive selection of transgenic plants

Cited by 29 publications

References 10 publications

Defense against Reactive Carbonyl Species Involves at Least Three Subcellular Compartments Where Individual Components of the System Respond to Cellular Sugar Status

Defense against Reactive Carbonyl Species Involves at Least Three Subcellular Compartments Where Individual Components of the System Respond to Cellular Sugar Status

The ancestors of diatoms evolved a unique mitochondrial dehydrogenase to oxidize photorespiratory glycolate

D-Lactate dehydrogenase links methylglyoxal degradation and electron transport through cytochrome C

Contact Info

Product

Resources

About