Dissecting the Physiological Function of Plant Glyoxalase I and Glyoxalase I-Like Proteins

Schmitz, J. E.; Rossoni, Alessandro W.; Maurino, Verónica G.

doi:10.3389/fpls.2018.01618

Cited by 24 publications

(35 citation statements)

References 45 publications

(60 reference statements)

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“…The other category of proteins comprised of functionally diverse and possibly inactive GLYI-like proteins. Schmitz et al [27] have recently proposed the occurrence of functional divergence in the Arabidopsis glyoxalase family. In Arabidopsis, eight proteins were reported to be the members of the GLYI-like category of proteins which lacked conserved motifs and shared only 17-21% sequence identity to AtGLYI-2, the Zn 2+ -dependent form.…”

Section: Discussionmentioning

confidence: 99%

“…Their biological activity is yet to be elucidated and even no close bacterial homologs have been identified to date. Importantly, Schmitz et al [27] also pointed that the phylogenetic occurrence of GLYI-like proteins is restricted to bacteria and the green lineage.…”

Section: Discussionmentioning

confidence: 99%

“…Overall, these GLYI protein encoding genes were predicted to be orthologous, and functionally similar. The third cluster contained greater number of proteins which have probably diverged in their functions and hence, were named as GLYI-like proteins [27].…”

Section: Phylogenetic Analysis Of Glyoxalase Proteins Of Sorghum and mentioning

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: Discussionmentioning

confidence: 99%

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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“…In our artificial self-incompatible Sha A. thaliana (Figure 5A), the pollen ligand AlSCRb is recognized by AlSRKb. As AlSRKb is phosphorylated and activated, it in turn activates AlARC1 which targets downstream factors including AtGLX1 for degradation by ubiquitination (Sankaranarayanan et al 2017;Schmitz et al 2018). The AtGLX1 levels then decrease and more proteins become MG-modified helping in the self-incompatible pollen response.…”

Section: Discussionmentioning

confidence: 99%

“…To determine pollen grain adherence to stigmas, the total number of pollen grains were tallied for three different images. The seed set data was graphed and analyzed using R-Studio Version 1.1.463 (2009-2018. The graph was generated using the ggplot2 package.…”

Section: Genotyping Of Transgenic Lines: Thementioning

confidence: 99%

Expression of Brassica napus GLO1 is sufficient to breakdown artificial self-incompatibility in Arabidopsis thaliana

Kenney

Sankaranarayanan

Balogh

et al. 2020

Preprint

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Members of the Brassicaceae family have the ability to regulate pollination events occurring on the stigma surface. In Brassica species, self-pollination leads to an allele specific interaction between the pollen small cysteine-rich peptide ligand (SCR/SP11) and the stigmatic S-receptor kinase (SRK) that activates the E3 ubiquitin ligase ARC1 (Armadillo repeat-containing 1), resulting in proteasomal degradation of various compatibility factors including Glyoxalase I (GLO1) which is necessary for successful pollination. Suppression of GLO1 was sufficient to reduce compatibility, and overexpression of GLO1 in self-incompatible Brassica napus stigmas resulted in partial breakdown of the self-incompatibility response. Here, we verified if BnGLO1 could function as a compatibility factor in the artificial self-incompatibility system of Arabidopsis thaliana expressing AlSCRb, AlSRKb and AlARC1 proteins from A. lyrata. Overexpression of BnGLO1 is sufficient to breakdown self-incompatibility response in A. thaliana stigmas, suggesting that GLO1 functions as an inter-species compatibility factor. Therefore, GLO1 has an indisputable role as a compatibility factor in the stigma in regulating pollen attachment and pollen tube growth. Lastly, this study demonstrates the usefulness of an artificial self-incompatibility system in A. thaliana for interspecific self-incompatibility studies.

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Color recycling: metabolization of apocarotenoid degradation products suggests carbon regeneration via primary metabolic pathways

et al. 2022

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Key message Analysis of carotenoid-accumulating roots revealed that oxidative carotenoid degradation yields glyoxal and methylglyoxal. Our data suggest that these compounds are detoxified via the glyoxalase system and re-enter primary metabolic pathways. Abstract Carotenoid levels in plant tissues depend on the relative rates of synthesis and degradation. We recently identified redox enzymes previously known to be involved in the detoxification of fatty acid-derived reactive carbonyl species which were able to convert apocarotenoids into corresponding alcohols and carboxylic acids. However, their subsequent metabolization pathways remain unresolved. Interestingly, we found that carotenoid-accumulating roots have increased levels of glutathione, suggesting apocarotenoid glutathionylation to occur. In vitro and in planta investigations did not, however, support the occurrence of non-enzymatic or enzymatic glutathionylation of β-apocarotenoids. An alternative breakdown pathway is the continued oxidative degradation of primary apocarotenoids or their derivatives into the shortest possible oxidation products, namely glyoxal and methylglyoxal, which also accumulated in carotenoid-accumulating roots. In fact, combined transcriptome and metabolome analysis suggest that the high levels of glutathione are most probably required for detoxifying apocarotenoid-derived glyoxal and methylglyoxal via the glyoxalase pathway, yielding glycolate and d-lactate, respectively. Further transcriptome analysis suggested subsequent reactions involving activities associated with photorespiration and the peroxisome-specific glycolate/glyoxylate transporter. Finally, detoxified primary apocarotenoid degradation products might be converted into pyruvate which is possibly re-used for the synthesis of carotenoid biosynthesis precursors. Our findings allow to envision carbon recycling during carotenoid biosynthesis, degradation and re-synthesis which consumes energy, but partially maintains initially fixed carbon via re-introducing reactive carotenoid degradation products into primary metabolic pathways.

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Dissecting the Physiological Function of Plant Glyoxalase I and Glyoxalase I-Like Proteins

Cited by 24 publications

References 45 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

Expression of Brassica napus GLO1 is sufficient to breakdown artificial self-incompatibility in Arabidopsis thaliana

Color recycling: metabolization of apocarotenoid degradation products suggests carbon regeneration via primary metabolic pathways

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