Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases
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...
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doaj-dcbd9ceff30440108c338fa2af99d67e2020-11-25T00:34:58ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2019-05-011010.3389/fpls.2019.00608452632Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione TransferasesElodie Sylvestre-Gonon0Simon R. Law1Mathieu Schwartz2Kevin Robe3Olivier Keech4Claude Didierjean5Christian Dubos6Nicolas Rouhier7Arnaud Hecker8Interactions Arbres-Microorganismes, Institut National de la Recherche Agronomique, Université de Lorraine, Nancy, FranceDepartment of Plant Physiology, Umeå Plant Science Centre, Umeå University, Umeå, SwedenCentre National de la Recherche Scientifique, Cristallographie, Résonance Magnétique et Modélisations, Université de Lorraine, Nancy, FranceBiochimie et Physiologie Moléculaire des Plantes (BPMP), INRA, CNRS, SupAgro-M, Université de Montpellier, Montpellier, FranceDepartment of Plant Physiology, Umeå Plant Science Centre, Umeå University, Umeå, SwedenCentre National de la Recherche Scientifique, Cristallographie, Résonance Magnétique et Modélisations, Université de Lorraine, Nancy, FranceBiochimie et Physiologie Moléculaire des Plantes (BPMP), INRA, CNRS, SupAgro-M, Université de Montpellier, Montpellier, FranceInteractions Arbres-Microorganismes, Institut National de la Recherche Agronomique, Université de Lorraine, Nancy, FranceInteractions Arbres-Microorganismes, Institut National de la Recherche Agronomique, Université de Lorraine, Nancy, FranceGlutathione 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.https://www.frontiersin.org/article/10.3389/fpls.2019.00608/fullphotosynthetic organismsphylogenystructureglutathione transferasesligandin propertysecondary metabolism |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Elodie Sylvestre-Gonon Simon R. Law Mathieu Schwartz Kevin Robe Olivier Keech Claude Didierjean Christian Dubos Nicolas Rouhier Arnaud Hecker |
spellingShingle |
Elodie Sylvestre-Gonon Simon R. Law Mathieu Schwartz Kevin Robe Olivier Keech Claude Didierjean Christian Dubos Nicolas Rouhier Arnaud Hecker Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases Frontiers in Plant Science photosynthetic organisms phylogeny structure glutathione transferases ligandin property secondary metabolism |
author_facet |
Elodie Sylvestre-Gonon Simon R. Law Mathieu Schwartz Kevin Robe Olivier Keech Claude Didierjean Christian Dubos Nicolas Rouhier Arnaud Hecker |
author_sort |
Elodie Sylvestre-Gonon |
title |
Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases |
title_short |
Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases |
title_full |
Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases |
title_fullStr |
Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases |
title_full_unstemmed |
Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases |
title_sort |
functional, structural and biochemical features of plant serinyl-glutathione transferases |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Plant Science |
issn |
1664-462X |
publishDate |
2019-05-01 |
description |
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. |
topic |
photosynthetic organisms phylogeny structure glutathione transferases ligandin property secondary metabolism |
url |
https://www.frontiersin.org/article/10.3389/fpls.2019.00608/full |
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