AtCXXS: atypical members of the Arabidopsis thaliana thioredoxin h family with a remarkably high disulfide isomerase activity.
Identifieur interne : 000C24 ( Main/Exploration ); précédent : 000C23; suivant : 000C25AtCXXS: atypical members of the Arabidopsis thaliana thioredoxin h family with a remarkably high disulfide isomerase activity.
Auteurs : Antonio Jesús Serrato [France] ; Jocelyne Guilleminot ; Yves Meyer ; Florence VignolsSource :
- Physiologia plantarum [ 1399-3054 ] ; 2008.
Descripteurs français
- KwdFr :
- Analyse de profil d'expression de gènes (MeSH), Analyse de séquence d'ADN (MeSH), Cytosol (métabolisme), Données de séquences moléculaires (MeSH), Phylogenèse (MeSH), Protein Disulfide-Isomerases (métabolisme), Protéines d'Arabidopsis (classification), Protéines d'Arabidopsis (génétique), Protéines d'Arabidopsis (métabolisme), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Protéines à fluorescence verte (génétique), Protéines à fluorescence verte (métabolisme), RT-PCR (MeSH), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Technique de Western (MeSH), Test de complémentation (MeSH), Thiorédoxine h (classification), Thiorédoxine h (génétique), Thiorédoxine h (métabolisme), Épissage alternatif (MeSH).
- MESH :
- classification : Protéines d'Arabidopsis, Thiorédoxine h.
- génétique : Protéines d'Arabidopsis, Protéines de fusion recombinantes, Protéines à fluorescence verte, Thiorédoxine h.
- métabolisme : Cytosol, Protein Disulfide-Isomerases, Protéines d'Arabidopsis, Protéines de fusion recombinantes, Protéines à fluorescence verte, Thiorédoxine h.
- Analyse de profil d'expression de gènes, Analyse de séquence d'ADN, Données de séquences moléculaires, Phylogenèse, RT-PCR, Similitude de séquences d'acides aminés, Séquence d'acides aminés, Technique de Western, Test de complémentation, Épissage alternatif.
English descriptors
- KwdEn :
- Alternative Splicing (MeSH), Amino Acid Sequence (MeSH), Arabidopsis Proteins (classification), Arabidopsis Proteins (genetics), Arabidopsis Proteins (metabolism), Blotting, Western (MeSH), Cytosol (metabolism), Gene Expression Profiling (MeSH), Genetic Complementation Test (MeSH), Green Fluorescent Proteins (genetics), Green Fluorescent Proteins (metabolism), Molecular Sequence Data (MeSH), Phylogeny (MeSH), Protein Disulfide-Isomerases (metabolism), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Reverse Transcriptase Polymerase Chain Reaction (MeSH), Sequence Analysis, DNA (MeSH), Sequence Homology, Amino Acid (MeSH), Thioredoxin h (classification), Thioredoxin h (genetics), Thioredoxin h (metabolism).
- MESH :
- chemical , classification : Arabidopsis Proteins, Thioredoxin h.
- chemical , genetics : Arabidopsis Proteins, Green Fluorescent Proteins, Recombinant Fusion Proteins, Thioredoxin h.
- chemical , metabolism : Arabidopsis Proteins, Green Fluorescent Proteins, Protein Disulfide-Isomerases, Recombinant Fusion Proteins, Thioredoxin h.
- metabolism : Cytosol.
- Alternative Splicing, Amino Acid Sequence, Blotting, Western, Gene Expression Profiling, Genetic Complementation Test, Molecular Sequence Data, Phylogeny, Reverse Transcriptase Polymerase Chain Reaction, Sequence Analysis, DNA, Sequence Homology, Amino Acid.
Abstract
The Arabidopsis thaliana thioredoxin subgroup h III is composed of four members and includes the two monocysteinic (CXXS) thioredoxins encoded by the genome. We show that AtCXXS1 is the ortholog of monocysteinic thioredoxins present in all higher plants. In contrast, unicellular algae and the moss Physcomitrella patens do not encode monocysteinic thioredoxin. AtCXXS2, the second monocysteinic thioredoxin of Arabidopsis has no ortholog in any other higher plants. It probably appeared recently by duplications of a dicysteinic thioredoxin of the same subgroup h III. Both monocysteinic thioredoxins show a low disulfide reductase activity in vitro but are very efficient as disulfide isomerases in RNAse refolding tests. The possible interactions of these proteins with the glutathione glutaredoxin pathway are discussed on the basis of recent papers.
DOI: 10.1111/j.1399-3054.2008.01093.x
PubMed: 18384502
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<term>Arabidopsis Proteins (genetics)</term>
<term>Arabidopsis Proteins (metabolism)</term>
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<term>Cytosol (metabolism)</term>
<term>Gene Expression Profiling (MeSH)</term>
<term>Genetic Complementation Test (MeSH)</term>
<term>Green Fluorescent Proteins (genetics)</term>
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<term>Molecular Sequence Data (MeSH)</term>
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<term>Recombinant Fusion Proteins (metabolism)</term>
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<term>Données de séquences moléculaires (MeSH)</term>
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<term>Thiorédoxine h (métabolisme)</term>
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<term>Phylogenèse</term>
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<term>Similitude de séquences d'acides aminés</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">The Arabidopsis thaliana thioredoxin subgroup h III is composed of four members and includes the two monocysteinic (CXXS) thioredoxins encoded by the genome. We show that AtCXXS1 is the ortholog of monocysteinic thioredoxins present in all higher plants. In contrast, unicellular algae and the moss Physcomitrella patens do not encode monocysteinic thioredoxin. AtCXXS2, the second monocysteinic thioredoxin of Arabidopsis has no ortholog in any other higher plants. It probably appeared recently by duplications of a dicysteinic thioredoxin of the same subgroup h III. Both monocysteinic thioredoxins show a low disulfide reductase activity in vitro but are very efficient as disulfide isomerases in RNAse refolding tests. The possible interactions of these proteins with the glutathione glutaredoxin pathway are discussed on the basis of recent papers.</div>
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<Abstract><AbstractText>The Arabidopsis thaliana thioredoxin subgroup h III is composed of four members and includes the two monocysteinic (CXXS) thioredoxins encoded by the genome. We show that AtCXXS1 is the ortholog of monocysteinic thioredoxins present in all higher plants. In contrast, unicellular algae and the moss Physcomitrella patens do not encode monocysteinic thioredoxin. AtCXXS2, the second monocysteinic thioredoxin of Arabidopsis has no ortholog in any other higher plants. It probably appeared recently by duplications of a dicysteinic thioredoxin of the same subgroup h III. Both monocysteinic thioredoxins show a low disulfide reductase activity in vitro but are very efficient as disulfide isomerases in RNAse refolding tests. The possible interactions of these proteins with the glutathione glutaredoxin pathway are discussed on the basis of recent papers.</AbstractText>
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