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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 : 000C25

AtCXXS: 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 Vignols

Source :

RBID : pubmed:18384502

Descripteurs français

English descriptors

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


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Le document en format XML

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<title xml:lang="en">AtCXXS: atypical members of the Arabidopsis thaliana thioredoxin h family with a remarkably high disulfide isomerase activity.</title>
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<term>Arabidopsis Proteins (genetics)</term>
<term>Arabidopsis Proteins (metabolism)</term>
<term>Blotting, Western (MeSH)</term>
<term>Cytosol (metabolism)</term>
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<term>Green Fluorescent Proteins (metabolism)</term>
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<term>Recombinant Fusion Proteins (genetics)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>Reverse Transcriptase Polymerase Chain Reaction (MeSH)</term>
<term>Sequence Analysis, DNA (MeSH)</term>
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<term>Protéines d'Arabidopsis (génétique)</term>
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<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<term>Test de complémentation (MeSH)</term>
<term>Thiorédoxine h (classification)</term>
<term>Thiorédoxine h (génétique)</term>
<term>Thiorédoxine h (métabolisme)</term>
<term>Épissage alternatif (MeSH)</term>
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<term>Phylogenèse</term>
<term>RT-PCR</term>
<term>Similitude de séquences d'acides aminés</term>
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<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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