GlutaredoxinV1, Main, Exploration, bibRecord, 000B61

The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation.

Identifieur interne : 000B61 ( Main/Exploration ); précédent : 000B60; suivant : 000B62

The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation.

Auteurs : Nicolas Rouhier [France] ; Stéphane D. Lemaire ; Jean-Pierre Jacquot

Source :

Annual review of plant biology [ 1543-5008 ] ; 2008.

RBID : pubmed:18444899

Descripteurs français

English descriptors

KwdEn :
- Glutaredoxins (metabolism), Glutathione (metabolism), Glutathione Transferase (metabolism), Oxidation-Reduction (MeSH), Photosynthesis (MeSH), Plant Physiological Phenomena (MeSH), Plant Proteins (metabolism), Plants (metabolism), Subcellular Fractions (metabolism).
MESH :
- chemical , metabolism : Glutaredoxins, Glutathione, Glutathione Transferase, Plant Proteins.
- metabolism : Plants, Subcellular Fractions.
- Oxidation-Reduction, Photosynthesis, Plant Physiological Phenomena.

Abstract

Glutathione, a tripeptide with the sequence gamma-Glu-Cys-Gly, exists either in a reduced form with a free thiol group or in an oxidized form with a disulfide between two identical molecules. We describe here briefly the pathways involved in the synthesis, reduction, polymerization, and degradation of glutathione, as well as its distribution throughout the plant and its redox buffering capacities. The function of glutathione in xenobiotic and heavy metal detoxification, plant development, and plant-pathogen interactions is also briefly discussed. Several lines of evidence indicate that glutathione and glutaredoxins (GRXs) are implicated in the response to oxidative stress through the regeneration of enzymes involved in peroxide and methionine sulfoxide reduction. Finally, emerging functions for plant GRXs and glutathione concern the regulation of protein activity via glutathionylation and the capacity of some GRXs to bind iron sulfur centers and for some of them to transfer FeS clusters into apoproteins.

DOI: 10.1146/annurev.arplant.59.032607.092811
PubMed: 18444899

Affiliations:

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Le document en format XML

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<affiliation wicri:level="3"><nlm:affiliation>Unité Mixte de Recherches, 1136 INRA-UHP Interaction Arbres-Microorganismes, IFR 110 GEEF, Nancy University, Faculté des Sciences, 54506 Vandoeuvre Cedex, France. nrouhier@scbiol.uhp-nancy.fr</nlm:affiliation>
<country xml:lang="fr">France</country>
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<term>Glutathione (metabolism)</term>
<term>Glutathione Transferase (metabolism)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Photosynthesis (MeSH)</term>
<term>Plant Physiological Phenomena (MeSH)</term>
<term>Plant Proteins (metabolism)</term>
<term>Plants (metabolism)</term>
<term>Subcellular Fractions (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Fractions subcellulaires (métabolisme)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Glutathion (métabolisme)</term>
<term>Glutathione transferase (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Photosynthèse (MeSH)</term>
<term>Phénomènes physiologiques des plantes (MeSH)</term>
<term>Plantes (métabolisme)</term>
<term>Protéines végétales (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
<term>Glutathione</term>
<term>Glutathione Transferase</term>
<term>Plant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Plants</term>
<term>Subcellular Fractions</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fractions subcellulaires</term>
<term>Glutarédoxines</term>
<term>Glutathion</term>
<term>Glutathione transferase</term>
<term>Plantes</term>
<term>Protéines végétales</term>
</keywords>
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<term>Plant Physiological Phenomena</term>
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<front><div type="abstract" xml:lang="en">Glutathione, a tripeptide with the sequence gamma-Glu-Cys-Gly, exists either in a reduced form with a free thiol group or in an oxidized form with a disulfide between two identical molecules. We describe here briefly the pathways involved in the synthesis, reduction, polymerization, and degradation of glutathione, as well as its distribution throughout the plant and its redox buffering capacities. The function of glutathione in xenobiotic and heavy metal detoxification, plant development, and plant-pathogen interactions is also briefly discussed. Several lines of evidence indicate that glutathione and glutaredoxins (GRXs) are implicated in the response to oxidative stress through the regeneration of enzymes involved in peroxide and methionine sulfoxide reduction. Finally, emerging functions for plant GRXs and glutathione concern the regulation of protein activity via glutathionylation and the capacity of some GRXs to bind iron sulfur centers and for some of them to transfer FeS clusters into apoproteins.</div>
</front>
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<Month>07</Month>
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<DateRevised><Year>2013</Year>
<Month>11</Month>
<Day>21</Day>
</DateRevised>
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<PubDate><Year>2008</Year>
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<Title>Annual review of plant biology</Title>
<ISOAbbreviation>Annu Rev Plant Biol</ISOAbbreviation>
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<ArticleTitle>The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation.</ArticleTitle>
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Serveur d'exploration sur la glutarédoxine

The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation.

The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki