Silencing of D-Lactate Dehydrogenase Impedes Glyoxalase System and Leads to Methylglyoxal Accumulation and Growth Inhibition in Rice

An, Baoguang; Lan, Jie; Deng, Xiaolong; Chen, Silan; Ouyang, Cheng; Shi, Huiyun; Yang, Jing; Li, Yangsheng

doi:10.3389/fpls.2017.02071

Cited by 19 publications

(24 citation statements)

References 63 publications

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“…Mitochondria is one of the potential sites for MG production and detoxification, possibly favouring the cell in protection against oxidative damage. The predicted presence of SbDLDH proteins in the mitochondria is in fact, in agreement with the known mitochondrial localization of D-LDH proteins from rice and Arabidopsis [12][13][14]. Further, it is possible that these mitochondrial D-LDH enzymes might acquire their substrate from within the organelle as few functionally active GLYI (SbGLYI-7 and SbGLYI-14) and GLYII (SbGLYII-4) proteins were also predicted to be present within the mitochondria (Fig.…”

Section: Discussionsupporting

confidence: 82%

“…However, no previous studies, ever reported the status of D-LDH proteins in plants. Experimental evidence suggests a crucial role of NADH-independent D-LDH proteins in the MG detoxification pathway which constitutes the last step of this process [12][13][14].…”

Section: Discussionmentioning

confidence: 99%

“…Further, GLYI and D-LDH from Arabidopsis have been shown to confer tolerance to various abiotic stresses in both prokaryotes and eukaryotes [13]. In rice, silencing of D-LDH impedes glyoxalase system leading to MG accumulation and growth inhibition [14].…”

Section: Introductionmentioning

confidence: 99%

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From methylglyoxal to pyruvate: a genome-wide study for the identification of glyoxalases and D-lactate dehydrogenases in Sorghum bicolor

et al. 2020

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Background: The glyoxalase pathway is evolutionarily conserved and involved in the glutathione-dependent detoxification of methylglyoxal (MG), a cytotoxic by-product of glycolysis. It acts via two metallo-enzymes, glyoxalase I (GLYI) and glyoxalase II (GLYII), to convert MG into D-lactate, which is further metabolized to pyruvate by D-lactate dehydrogenases (D-LDH). Since D-lactate formation occurs solely by the action of glyoxalase enzymes, its metabolism may be considered as the ultimate step of MG detoxification. By maintaining steady state levels of MG and other reactive dicarbonyl compounds, the glyoxalase pathway serves as an important line of defence against glycation and oxidative stress in living organisms. Therefore, considering the general role of glyoxalases in stress adaptation and the ability of Sorghum bicolor to withstand prolonged drought, the sorghum glyoxalase pathway warrants an in-depth investigation with regard to the presence, regulation and distribution of glyoxalase and D-LDH genes. Result: Through this study, we have identified 15 GLYI and 6 GLYII genes in sorghum. In addition, 4 D-LDH genes were also identified, forming the first ever report on genome-wide identification of any plant D-LDH family. Our in silico analysis indicates homology of putatively active SbGLYI, SbGLYII and SbDLDH proteins to several functionally characterised glyoxalases and D-LDHs from Arabidopsis and rice. Further, these three gene families exhibit development and tissue-specific variations in their expression patterns. Importantly, we could predict the distribution of putatively active SbGLYI, SbGLYII and SbDLDH proteins in at least four different sub-cellular compartments namely, cytoplasm, chloroplast, nucleus and mitochondria. Most of the members of the sorghum glyoxalase and D-LDH gene families are indeed found to be highly stress responsive.Conclusion: This study emphasizes the role of glyoxalases as well as that of D-LDH in the complete detoxification of MG in sorghum. In particular, we propose that D-LDH which metabolizes the specific end product of glyoxalases pathway is essential for complete MG detoxification. By proposing a cellular model for detoxification of MG via glyoxalase pathway in sorghum, we suggest that different sub-cellular organelles are actively involved in MG metabolism in plants.

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Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 99%

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From methylglyoxal to pyruvate: a genome-wide study for the identification of glyoxalases and D-lactate dehydrogenases in Sorghum bicolor

et al. 2020

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“…The first is the GSH-dependent glyoxalase pathway; the second pathway involves glyoxalase enzyme Gly III (DJ-1), which converts MG to D-lactate in a single step without the intermediate processes 18 . In the GSH-dependent glyoxalase pathway, Gly I is the first enzyme which catalyzes the isomerization of MG into S-2-hydroxyacylglutathione and then Gly II hydrolyzes these thiolesters to produce D-lactate, which will eventually be converted into pyruvate to feed into tricarboxylic acid (TCA) cycle [19][20][21] . Since its initial characterization of the glyoxalase pathway back in 1913 22,23 , the importance of the glyoxalase system in plant defense against various types of biotic and abiotic stresses has been more and more firmly recognized 24,25 .…”

Section: Introductionmentioning

confidence: 99%

Al-induced proteomics changes in tomato plants over-expressing a glyoxalase I gene

Thapa

et al. 2020

Hortic Res

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Glyoxalase I (Gly I) is the first enzyme in the glutathionine-dependent glyoxalase pathway for detoxification of methylglyoxal (MG) under stress conditions. Transgenic tomato 'Money Maker' plants overexpressing tomato SlGlyI gene (tomato unigene accession SGN-U582631/Solyc09g082120.3.1) were generated and homozygous lines were obtained after four generations of self-pollination. In this study, SlGlyI-overepxressing line (GlyI), wild type (WT, negative control) and plants transformed with empty vector (ECtr, positive control), were subjected to Al-treatment by growing in Magnavaca's nutrient solution (pH 4.5) supplemented with 20 µM Al 3+ ion activity. After 30 days of treatments, the fresh and dry weight of shoots and roots of plants from Al-treated conditions decreased significantly compared to the non-treated conditions for all the three lines. When compared across the three lines, root fresh and dry weight of GlyI was significant higher than WT and ECtr, whereas there was no difference in shoot tissues. The basal 5 mm root-tips of GlyI plants expressed a significantly higher level of glyoxalase activity under both non-Al-treated and Al-treated conditions compared to the two control lines. Under Al-treated condition, there was a significant increase in MG content in ECtr and WT lines, but not in GlyI line. Quantitative proteomics analysis using tandem mass tags mass spectrometry identified 4080 quantifiable proteins and 201 Al-induced differentially expressed proteins (DEPs) in roottip tissues from GlyI, and 4273 proteins and 230 DEPs from ECtr. The Al-down-regulated DEPs were classified into molecular pathways of gene transcription, RNA splicing and protein biosynthesis in both GlyI and ECtr lines. The Alinduced DEPs in GlyI associated with tolerance to Al 3+ and MG toxicity are involved in callose degradation, cell wall components (xylan acetylation and pectin degradation), oxidative stress (antioxidants) and turnover of Al-damaged epidermal cells, repair of damaged DNA, epigenetics, gene transcription, and protein translation. A protein-protein association network was constructed to aid the selection of proteins in the same pathway but differentially regulated in GlyI or ECtr lines. Proteomics data are available via ProteomeXchange with identifiers PXD009456 under project title '25Dec2017_Suping_XSexp2_ITAG3.2' for SlGlyI-overexpressing tomato plants and PXD009848 under project title '25Dec2017_Suping_XSexp3_ITAG3.2' for positive control ECtr line transformed with empty vector.

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“…In plants, the role of mitochondrial LDH on plant defence and ROS production is largely unexplored. Diverse plant species such as Arabidopsis, rice, and Jerusalem artichoke possess not only L‐LDH, but also D‐LDH, which oxidizes d ‐lactate (Atlante et al , ; Welchen et al , ; An et al , ). Based on previous reports on ROS production by l ‐lactic acid in animal cells, we hypothesized that exogenous d ‐lactic acid induces ROS production in Arabidopsis via the oxidation of d ‐lactate by d ‐LDH.…”

Section: Discussionmentioning

confidence: 99%

d‐Lactic acid secreted by Chlorella fusca primes pattern‐triggered immunity against Pseudomonas syringae in Arabidopsis

et al. 2020

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Biological control agents including microbes and their products have been studied as sustainable crop protection strategies. Although aquatic microalgae have been recently introduced as a biological control agent, the underlying molecular mechanisms are largely unknown. The aim of the present study was to investigate the molecular mechanisms underlying biological control by microalga Chlorella fusca. Foliar application of C. fusca elicits induced resistance in Arabidopsis thaliana against Pseudomonas syringae pv. tomato DC3000 that activates plant immunity rather than direct antagonism. To understand the basis of C. fuscatriggered induced resistance at the transcriptional level, we conducted RNA sequencing (RNA-seq) analysis. RNA-seq data showed that, upon pathogen inoculation, C. fusca treatment primed the expression of cysteine-rich receptor-like kinases, WRKY transcription factor genes, and salicylic acid and jasmonic acid signalling-related genes. Intriguingly, the application of C. fusca primed pathogen-associated molecular pattern -triggered immunity, characterized by reactive oxygen species burst and callose deposition, upon flagellin 22 treatment. The attempts to find C. fusca determinants allowed us to identify D-lactic acid secreted in the supernatant of C. fusca as a defence priming agent. This is the first report of the mechanism of innate immune activation by aquatic microalga Chlorella in higher plants.

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Silencing of D-Lactate Dehydrogenase Impedes Glyoxalase System and Leads to Methylglyoxal Accumulation and Growth Inhibition in Rice

Cited by 19 publications

References 63 publications

From methylglyoxal to pyruvate: a genome-wide study for the identification of glyoxalases and D-lactate dehydrogenases in Sorghum bicolor

From methylglyoxal to pyruvate: a genome-wide study for the identification of glyoxalases and D-lactate dehydrogenases in Sorghum bicolor

Al-induced proteomics changes in tomato plants over-expressing a glyoxalase I gene

d‐Lactic acid secreted by Chlorella fusca primes pattern‐triggered immunity against Pseudomonas syringae in Arabidopsis

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