Structure, Evolution and Functional Roles of Plant Glutathione Transferases

Chronopoulou, Evangelia; Ataya, Farid S.; Pouliou, Fotini; Perperopoulou, Fereniki; Georgakis, Nikolaos; Nianiou-Obeidat, Irini; Madesis, Panagiotis; Ioannou, Elisavet; Labrou, Nikolaos E.

doi:10.1007/978-3-319-66682-2_9

Cited by 12 publications

(17 citation statements)

References 100 publications

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“…The rapid formation of GSH conjugates suggests catalysis by GSTs, a mostly cytosolic enzyme family, causing enhanced flufenacet detoxification resulting in resistance. Similar results have been obtained in recurrently selected pyroxasulfone‐resistant L. rigidum from Australia, in which pyroxasulfone–GSH conjugates were detected, indicating enhanced GST‐catalyzed detoxification …”

Section: Discussionmentioning

confidence: 99%

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Glutathione transferase plays a major role in flufenacet resistance of ryegrass (Lolium spp.) field populations

Dücker

Zöllner

Lümmen

et al. 2019

Pest Management Science

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BACKGROUND: Herbicides inhibiting the synthesis of very long-chain fatty acids (HRAC group K 3 , WSSA group 15), such as flufenacet, play an important role in weed management strategies, particularly when herbicide resistance to inhibitors with other modes of action, such as acetolactate synthase or acetyl coenzyme A carboxylase (ACCase), has already evolved. So far, only a few cases of resistance towards inhibitors of the synthesis of very long-chain fatty acids have been described. In this study, we characterized the level of flufenacet resistance in several Lolium spp. field populations and investigated the resistance mechanism. RESULTS: The screening for flufenacet resistance revealed the ability of Lolium spp. populations from several continents to survive flufenacet treatments at and above the field rate. This study demonstrates the way in which flufenacet is detoxified in resistant weed populations. Glutathione was found to be conjugated to flufenacet in Lolium spp. seedlings, and there was evidence that glutathione transferase activity was enhanced in protein extracts from flufenacet-resistant seedlings. A significant correlation was found between the resistance factor obtained by biotests and the degradation half-time of flufenacet in ryegrass plants obtained by high-performance liquid chromatography (HPLC). CONCLUSION: At present, flufenacet resistance is not widespread; however, in certain Lolium spp. populations resistance levels could reach agronomic relevance due to detoxification by glutathione transferases. In Europe especially, only a few herbicide modes of action are registered for the control of Lolium spp. and therefore it is becoming increasingly important to apply best management practices to prevent the spread of flufenacet resistance.

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Section: Discussionmentioning

confidence: 99%

“…The metabolites M371, M443 and M314 accumulating in extracts of flufenacet‐resistant Lolium biotypes may have resulted from further cleavage of flufenacet–GSH conjugate by vacuolar peptidases after vacuolar sequestration . Additionally, several phase III metabolites were detected in the plant extracts.…”

Section: Discussionmentioning

confidence: 99%

Glutathione transferase plays a major role in flufenacet resistance of ryegrass (Lolium spp.) field populations

Dücker

Zöllner

Lümmen

et al. 2019

Pest Management Science

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“…GSTs are versatile enzymes, accommodating diverse substrates/ligands in the active site or L-sites (Table 2), and catalyzing diverse enzymatic reactions as a function of the active site signature (Chronopoulou et al, 2017a). Besides the so-called ligandin function, Ser-GSTs catalyze GSH-conjugation reactions on numerous types of substrates, the reduction of organic hydroperoxides or substrate isomerisation whereas Cys-GSTs rather catalyze opposite reactions including the reduction of glutathione conjugates.…”

Section: Introductionmentioning

confidence: 99%

Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases

et al. 2019

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Glutathione transferases (GSTs) belong to a ubiquitous multigenic family of enzymes involved in diverse biological processes including xenobiotic detoxification and secondary metabolism. A canonical GST is formed by two domains, the N-terminal one adopting a thioredoxin (TRX) fold and the C-terminal one an all-helical structure. The most recent genomic and phylogenetic analysis based on this domain organization allowed the classification of the GST family into 14 classes in terrestrial plants. These GSTs are further distinguished based on the presence of the ancestral cysteine (Cys-GSTs) present in TRX family proteins or on its substitution by a serine (Ser-GSTs). Cys-GSTs catalyze the reduction of dehydroascorbate and deglutathionylation reactions whereas Ser-GSTs catalyze glutathione conjugation reactions and eventually have peroxidase activity, both activities being important for stress tolerance or herbicide detoxification. Through non-catalytic, so-called ligandin properties, numerous plant GSTs also participate in the binding and transport of small heterocyclic ligands such as flavonoids including anthocyanins, and polyphenols. So far, this function has likely been underestimated compared to the other documented roles of GSTs. In this review, we compiled data concerning the known enzymatic and structural properties as well as the biochemical and physiological functions associated to plant GSTs having a conserved serine in their active site.

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“…Among all the cDEGs, 13 genes (24.1%) were denoted as enzyme genes using a combinational annotation of KEGG, NR and Swiss-Prot databases. These enzyme genes, such as serine carboxypeptidase, glutamate synthase and glutathione S -transferase, were reported to be related to plant secondary metabolism in the previous studies [ 39 – 41 ]. We also found a number of TF genes (e.g., NAC , bZIP ) that may act as regulatory switches in thea biosynthesis.…”

Section: Resultsmentioning

confidence: 99%

Time-series transcriptomic analysis reveals novel gene modules that control theanine biosynthesis in tea plant (Camellia sinensis)

Cao

et al. 2020

PLoS ONE

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Theanine (thea) is a unique non-protein amino acid in tea plant (Camellia sinensis) and one of the most important small molecular compounds for tea quality and health effects. The molecular mechanism that maintains thea biosynthesis is not clear but may be reflected in complicated biological networks as other secondary metabolites in plants. We performed an integrative transcriptomic analysis of tea seedlings bud and leave over the time-course of ethylamine (EA) treatment that activated thea pathway. We identified 54 consistent differentially expressed genes (cDEGs, 25 upregulated and 29 downregulated) during thea activation. Gene Ontology (GO) functional enrichment analysis of upregulated genes and downregulated genes showed that they may function as a cascade of biological events during their cooperative contribution to thea biosynthesis. Among the total cDEGs, a diversity of functional genes (e.g., enzymes, transcription factors, transport and binding proteins) were identified, indicating a hierarchy of gene control network underlying thea biosynthesis. A gene network associated with thea biosynthesis was modeled and three interconnected gene functional modules were identified. Among the gene modules, several topologically important genes (e.g., CsBCS-1, CsRP, CsABC2) were experimentally validated using a combined thea content and gene expression analysis. Collectively, we presented here for the first time a comprehensive landscape of the biosynthetic mechanism of thea controlled by a underling gene network, which might provide a theoretical basis for the identification of key genes that contribute to thea biosynthesis.

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Structure, Evolution and Functional Roles of Plant Glutathione Transferases

Cited by 12 publications

References 100 publications

Glutathione transferase plays a major role in flufenacet resistance of ryegrass (Lolium spp.) field populations

Glutathione transferase plays a major role in flufenacet resistance of ryegrass (Lolium spp.) field populations

Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases

Time-series transcriptomic analysis reveals novel gene modules that control theanine biosynthesis in tea plant (Camellia sinensis)

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