Redox regulation in photosynthetic organisms: focus on glutathionylation.
Identifieur interne : 000823 ( Main/Exploration ); précédent : 000822; suivant : 000824Redox regulation in photosynthetic organisms: focus on glutathionylation.
Auteurs : Mirko Zaffagnini [France] ; Mariette Bedhomme ; Christophe H. Marchand ; Samuel Morisse ; Paolo Trost ; Stéphane D. LemaireSource :
- Antioxidants & redox signaling [ 1557-7716 ] ; 2012.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Glutathion, Protéines.
- Animaux, Humains, Oxydoréduction, Photosynthèse.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Glutathione, Proteins.
- Animals, Humans, Oxidation-Reduction, Photosynthesis.
Abstract
SIGNIFICANCE
In photosynthetic organisms, besides the well-established disulfide/dithiol exchange reactions specifically controlled by thioredoxins (TRXs), protein S-glutathionylation is emerging as an alternative redox modification occurring under stress conditions. This modification, consisting of the formation of a mixed disulfide between glutathione and a protein cysteine residue, can not only protect specific cysteines from irreversible oxidation but also modulate protein activities and appears to be specifically controlled by small disulfide oxidoreductases of the TRX superfamily named glutaredoxins (GRXs).
RECENT STUDIES
In recent times, several studies allowed significant progress in this area, mostly due to the identification of several plant proteins undergoing S-glutathionylation and to the characterization of the molecular mechanisms and the proteins involved in the control of this modification.
CRITICAL ISSUES
This article provides a global overview of protein glutathionylation in photosynthetic organisms with particular emphasis on the mechanisms of protein glutathionylation and deglutathionylation and a focus on the role of GRXs. Then, we describe the methods employed for identification of glutathionylated proteins in photosynthetic organisms and review the targets and the possible physiological functions of protein glutathionylation.
FUTURE DIRECTIONS
In order to establish the importance of protein S-glutathionylation in photosynthetic organisms, future studies should be aimed at delineating more accurately the molecular mechanisms of glutathionylation and deglutathionylation reactions, at identifying proteins undergoing S-glutathionylation in vivo under diverse conditions, and at investigating the importance of redoxins, GRX, and TRX, in the control of this redox modification in vivo.
DOI: 10.1089/ars.2011.4255
PubMed: 22053845
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<term>Photosynthesis (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Glutathion (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Photosynthèse (MeSH)</term>
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<front><div type="abstract" xml:lang="en"><p><b>SIGNIFICANCE</b>
</p>
<p>In photosynthetic organisms, besides the well-established disulfide/dithiol exchange reactions specifically controlled by thioredoxins (TRXs), protein S-glutathionylation is emerging as an alternative redox modification occurring under stress conditions. This modification, consisting of the formation of a mixed disulfide between glutathione and a protein cysteine residue, can not only protect specific cysteines from irreversible oxidation but also modulate protein activities and appears to be specifically controlled by small disulfide oxidoreductases of the TRX superfamily named glutaredoxins (GRXs).</p>
</div>
<div type="abstract" xml:lang="en"><p><b>RECENT STUDIES</b>
</p>
<p>In recent times, several studies allowed significant progress in this area, mostly due to the identification of several plant proteins undergoing S-glutathionylation and to the characterization of the molecular mechanisms and the proteins involved in the control of this modification.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>CRITICAL ISSUES</b>
</p>
<p>This article provides a global overview of protein glutathionylation in photosynthetic organisms with particular emphasis on the mechanisms of protein glutathionylation and deglutathionylation and a focus on the role of GRXs. Then, we describe the methods employed for identification of glutathionylated proteins in photosynthetic organisms and review the targets and the possible physiological functions of protein glutathionylation.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>FUTURE DIRECTIONS</b>
</p>
<p>In order to establish the importance of protein S-glutathionylation in photosynthetic organisms, future studies should be aimed at delineating more accurately the molecular mechanisms of glutathionylation and deglutathionylation reactions, at identifying proteins undergoing S-glutathionylation in vivo under diverse conditions, and at investigating the importance of redoxins, GRX, and TRX, in the control of this redox modification in vivo.</p>
</div>
</front>
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