GlutaredoxinV1, Main, Exploration, bibRecord, 000C39

Thioredoxins in chloroplasts.

Identifieur interne : 000C39 ( Main/Exploration ); précédent : 000C38; suivant : 000C40

Thioredoxins in chloroplasts.

Auteurs : Stéphane D. Lemaire [France] ; Laure Michelet ; Mirko Zaffagnini ; Vincent Massot ; Emmanuelle Issakidis-Bourguet

Source :

Current genetics [ 0172-8083 ] ; 2007.

RBID : pubmed:17431629

Descripteurs français

KwdFr :
- Alignement de séquences (MeSH), Animaux (MeSH), Chloroplastes (composition chimique), Chloroplastes (enzymologie), Glutarédoxines (MeSH), Glutathion (métabolisme), Isoformes de protéines (MeSH), Masse moléculaire (MeSH), Modèles biologiques (MeSH), Oxidoreductases (composition chimique), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Protéines végétales (composition chimique), Protéines végétales (métabolisme), Protéomique (MeSH), Thiorédoxines (composition chimique), Thiorédoxines (génétique), Thiorédoxines (métabolisme), Transduction du signal (physiologie), Voies et réseaux métaboliques (MeSH).
MESH :
- composition chimique : Chloroplastes, Oxidoreductases, Protéines végétales, Thiorédoxines.
- enzymologie : Chloroplastes.
- génétique : Oxidoreductases, Thiorédoxines.
- métabolisme : Glutathion, Oxidoreductases, Protéines végétales, Thiorédoxines.
- physiologie : Transduction du signal.
- Alignement de séquences, Animaux, Glutarédoxines, Isoformes de protéines, Masse moléculaire, Modèles biologiques, Oxydoréduction, Protéomique, Voies et réseaux métaboliques.

English descriptors

KwdEn :
- Animals (MeSH), Chloroplasts (chemistry), Chloroplasts (enzymology), Glutaredoxins (MeSH), Glutathione (metabolism), Metabolic Networks and Pathways (MeSH), Models, Biological (MeSH), Molecular Weight (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (chemistry), Oxidoreductases (genetics), Oxidoreductases (metabolism), Plant Proteins (chemistry), Plant Proteins (metabolism), Protein Isoforms (MeSH), Proteomics (MeSH), Sequence Alignment (MeSH), Signal Transduction (physiology), Thioredoxins (chemistry), Thioredoxins (genetics), Thioredoxins (metabolism).
MESH :
- chemical , chemistry : Oxidoreductases, Plant Proteins, Thioredoxins.
- chemical , genetics : Oxidoreductases, Thioredoxins.
- chemical , metabolism : Glutathione, Oxidoreductases, Plant Proteins, Thioredoxins.
- chemical : Glutaredoxins, Protein Isoforms.
- chemistry : Chloroplasts.
- enzymology : Chloroplasts.
- physiology : Signal Transduction.
- Animals, Metabolic Networks and Pathways, Models, Biological, Molecular Weight, Oxidation-Reduction, Proteomics, Sequence Alignment.

Abstract

Thioredoxins (TRXs) are small disulfide oxidoreductases of ca. 12 kDa found in all free living organisms. In plants, two chloroplastic TRXs, named TRX f and TRX m, were originally identified as light dependent regulators of several carbon metabolism enzymes including Calvin cycle enzymes. The availability of genome sequences revealed an unsuspected multiplicity of TRXs in photosynthetic eukaryotes, including new chloroplastic TRX types. Moreover, proteomic approaches and focused studies allowed identification of 90 potential chloroplastic TRX targets. Lately, recent studies suggest the existence of a complex interplay between TRXs and other redox regulators such as glutaredoxins (GRXs) or glutathione. The latter is involved in a post-translational modification, named glutathionylation that could be controlled by GRXs. Glutathionylation appears to specifically affect the activity of TRX f and other chloroplastic enzymes and could thereby constitute a previously undescribed regulatory mechanism of photosynthetic metabolism under oxidative stress. After summarizing the initial studies on TRX f and TRX m, this review will focus on the most recent developments with special emphasis on the contributions of genomics and proteomics to the field of TRXs. Finally, new emerging interactions with other redox signaling pathways and perspectives for future studies will also be discussed.

DOI: 10.1007/s00294-007-0128-z
PubMed: 17431629

Affiliations:

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

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Le document en format XML

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<term>Glutaredoxins (MeSH)</term>
<term>Glutathione (metabolism)</term>
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<term>Models, Biological (MeSH)</term>
<term>Molecular Weight (MeSH)</term>
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<term>Oxidoreductases (genetics)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Plant Proteins (chemistry)</term>
<term>Plant Proteins (metabolism)</term>
<term>Protein Isoforms (MeSH)</term>
<term>Proteomics (MeSH)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Signal Transduction (physiology)</term>
<term>Thioredoxins (chemistry)</term>
<term>Thioredoxins (genetics)</term>
<term>Thioredoxins (metabolism)</term>
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<term>Oxidoreductases (métabolisme)</term>
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<term>Protéines végétales (métabolisme)</term>
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<term>Thiorédoxines (génétique)</term>
<term>Thiorédoxines (métabolisme)</term>
<term>Transduction du signal (physiologie)</term>
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<term>Masse moléculaire</term>
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<front><div type="abstract" xml:lang="en">Thioredoxins (TRXs) are small disulfide oxidoreductases of ca. 12 kDa found in all free living organisms. In plants, two chloroplastic TRXs, named TRX f and TRX m, were originally identified as light dependent regulators of several carbon metabolism enzymes including Calvin cycle enzymes. The availability of genome sequences revealed an unsuspected multiplicity of TRXs in photosynthetic eukaryotes, including new chloroplastic TRX types. Moreover, proteomic approaches and focused studies allowed identification of 90 potential chloroplastic TRX targets. Lately, recent studies suggest the existence of a complex interplay between TRXs and other redox regulators such as glutaredoxins (GRXs) or glutathione. The latter is involved in a post-translational modification, named glutathionylation that could be controlled by GRXs. Glutathionylation appears to specifically affect the activity of TRX f and other chloroplastic enzymes and could thereby constitute a previously undescribed regulatory mechanism of photosynthetic metabolism under oxidative stress. After summarizing the initial studies on TRX f and TRX m, this review will focus on the most recent developments with special emphasis on the contributions of genomics and proteomics to the field of TRXs. Finally, new emerging interactions with other redox signaling pathways and perspectives for future studies will also be discussed.</div>
</front>
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<Abstract><AbstractText>Thioredoxins (TRXs) are small disulfide oxidoreductases of ca. 12 kDa found in all free living organisms. In plants, two chloroplastic TRXs, named TRX f and TRX m, were originally identified as light dependent regulators of several carbon metabolism enzymes including Calvin cycle enzymes. The availability of genome sequences revealed an unsuspected multiplicity of TRXs in photosynthetic eukaryotes, including new chloroplastic TRX types. Moreover, proteomic approaches and focused studies allowed identification of 90 potential chloroplastic TRX targets. Lately, recent studies suggest the existence of a complex interplay between TRXs and other redox regulators such as glutaredoxins (GRXs) or glutathione. The latter is involved in a post-translational modification, named glutathionylation that could be controlled by GRXs. Glutathionylation appears to specifically affect the activity of TRX f and other chloroplastic enzymes and could thereby constitute a previously undescribed regulatory mechanism of photosynthetic metabolism under oxidative stress. After summarizing the initial studies on TRX f and TRX m, this review will focus on the most recent developments with special emphasis on the contributions of genomics and proteomics to the field of TRXs. Finally, new emerging interactions with other redox signaling pathways and perspectives for future studies will also be discussed.</AbstractText>
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<ForeName>Vincent</ForeName>
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<Author ValidYN="Y"><LastName>Issakidis-Bourguet</LastName>
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Thioredoxins in chloroplasts.

Thioredoxins in chloroplasts.

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