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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Main Authors: Elodie Sylvestre-Gonon, Simon R. Law, Mathieu Schwartz, Kevin Robe, Olivier Keech, Claude Didierjean, Christian Dubos, Nicolas Rouhier, Arnaud Hecker
Format: Article
Language:English
Published: Frontiers Media S.A. 2019-05-01
Series:Frontiers in Plant Science
Subjects:
Online Access:https://www.frontiersin.org/article/10.3389/fpls.2019.00608/full
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spelling 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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