PoplarV1, Main, Exploration, bibRecord, 003A05

A novel type of thioredoxin dedicated to symbiosis in legumes.

Identifieur interne : 003A05 ( Main/Exploration ); précédent : 003A04; suivant : 003A06

A novel type of thioredoxin dedicated to symbiosis in legumes.

Auteurs : Fatima Alkhalfioui [France] ; Michelle Renard ; Pierre Frendo ; Corinne Keichinger ; Yves Meyer ; Eric Gelhaye ; Masakazu Hirasawa ; David B. Knaff ; Christophe Ritzenthaler ; Françoise Montrichard

Source :

Plant physiology [ 0032-0889 ] ; 2008.

RBID : pubmed:18614707

Descripteurs français

KwdFr :
- Animaux (MeSH), Anticorps (métabolisme), Arabidopsis (génétique), Arabidopsis (métabolisme), Données de séquences moléculaires (MeSH), Escherichia coli (génétique), Escherichia coli (métabolisme), Isoformes de protéines (MeSH), Lapins (MeSH), Medicago truncatula (physiologie), Réticulum endoplasmique (métabolisme), Symbiose (MeSH), Séquence d'acides aminés (MeSH), Thioredoxin-disulfide reductase (métabolisme), Thiorédoxines (physiologie).
MESH :
- génétique : Arabidopsis, Escherichia coli.
- métabolisme : Anticorps, Arabidopsis, Escherichia coli, Réticulum endoplasmique, Thioredoxin-disulfide reductase.
- physiologie : Medicago truncatula, Thiorédoxines.
- Animaux, Données de séquences moléculaires, Isoformes de protéines, Lapins, Symbiose, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Antibodies (metabolism), Arabidopsis (genetics), Arabidopsis (metabolism), Endoplasmic Reticulum (metabolism), Escherichia coli (genetics), Escherichia coli (metabolism), Medicago truncatula (physiology), Molecular Sequence Data (MeSH), Protein Isoforms (MeSH), Rabbits (MeSH), Symbiosis (MeSH), Thioredoxin-Disulfide Reductase (metabolism), Thioredoxins (physiology).
MESH :
- chemical , metabolism : Antibodies, Thioredoxin-Disulfide Reductase.
- genetics : Arabidopsis, Escherichia coli.
- metabolism : Arabidopsis, Endoplasmic Reticulum, Escherichia coli.
- physiology : Medicago truncatula, Thioredoxins.
- Amino Acid Sequence, Animals, Molecular Sequence Data, Protein Isoforms, Rabbits, Symbiosis.

Abstract

Thioredoxins (Trxs) constitute a family of small proteins in plants. This family has been extensively characterized in Arabidopsis (Arabidopsis thaliana), which contains six different Trx types: f, m, x, and y in chloroplasts, o in mitochondria, and h mainly in cytosol. A detailed study of this family in the model legume Medicago truncatula, realized here, has established the existence of two isoforms that do not belong to any of the types previously described. As no possible orthologs were further found in either rice (Oryza sativa) or poplar (Populus spp.), these novel isoforms may be specific for legumes. Nevertheless, on the basis of protein sequence and gene structure, they are both related to Trxs m and probably have evolved from Trxs m after the divergence of the higher plant families. They have redox potential values similar to those of the classical Trxs, and one of them can act as a substrate for the M. truncatula NADP-Trx reductase A. However, they differ from classical Trxs in that they possess an atypical putative catalytic site and lack disulfide reductase activity with insulin. Another important feature is the presence in both proteins of an N-terminal extension containing a putative signal peptide that targets them to the endoplasmic reticulum, as demonstrated by their transient expression in fusion with the green fluorescent protein in M. truncatula or Nicotiana benthamiana leaves. According to their pattern of expression, these novel isoforms function specifically in symbiotic interactions in legumes. They were therefore given the name of Trxs s, s for symbiosis.

DOI: 10.1104/pp.108.123778
PubMed: 18614707
PubMed Central: PMC2528116

Affiliations:

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

to stream Main, to step Corpus: 003843
to stream Main, to step Curation: 003843

Le document en format XML

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<front><div type="abstract" xml:lang="en">Thioredoxins (Trxs) constitute a family of small proteins in plants. This family has been extensively characterized in Arabidopsis (Arabidopsis thaliana), which contains six different Trx types: f, m, x, and y in chloroplasts, o in mitochondria, and h mainly in cytosol. A detailed study of this family in the model legume Medicago truncatula, realized here, has established the existence of two isoforms that do not belong to any of the types previously described. As no possible orthologs were further found in either rice (Oryza sativa) or poplar (Populus spp.), these novel isoforms may be specific for legumes. Nevertheless, on the basis of protein sequence and gene structure, they are both related to Trxs m and probably have evolved from Trxs m after the divergence of the higher plant families. They have redox potential values similar to those of the classical Trxs, and one of them can act as a substrate for the M. truncatula NADP-Trx reductase A. However, they differ from classical Trxs in that they possess an atypical putative catalytic site and lack disulfide reductase activity with insulin. Another important feature is the presence in both proteins of an N-terminal extension containing a putative signal peptide that targets them to the endoplasmic reticulum, as demonstrated by their transient expression in fusion with the green fluorescent protein in M. truncatula or Nicotiana benthamiana leaves. According to their pattern of expression, these novel isoforms function specifically in symbiotic interactions in legumes. They were therefore given the name of Trxs s, s for symbiosis.</div>
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<Abstract><AbstractText>Thioredoxins (Trxs) constitute a family of small proteins in plants. This family has been extensively characterized in Arabidopsis (Arabidopsis thaliana), which contains six different Trx types: f, m, x, and y in chloroplasts, o in mitochondria, and h mainly in cytosol. A detailed study of this family in the model legume Medicago truncatula, realized here, has established the existence of two isoforms that do not belong to any of the types previously described. As no possible orthologs were further found in either rice (Oryza sativa) or poplar (Populus spp.), these novel isoforms may be specific for legumes. Nevertheless, on the basis of protein sequence and gene structure, they are both related to Trxs m and probably have evolved from Trxs m after the divergence of the higher plant families. They have redox potential values similar to those of the classical Trxs, and one of them can act as a substrate for the M. truncatula NADP-Trx reductase A. However, they differ from classical Trxs in that they possess an atypical putative catalytic site and lack disulfide reductase activity with insulin. Another important feature is the presence in both proteins of an N-terminal extension containing a putative signal peptide that targets them to the endoplasmic reticulum, as demonstrated by their transient expression in fusion with the green fluorescent protein in M. truncatula or Nicotiana benthamiana leaves. According to their pattern of expression, these novel isoforms function specifically in symbiotic interactions in legumes. They were therefore given the name of Trxs s, s for symbiosis.</AbstractText>
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A novel type of thioredoxin dedicated to symbiosis in legumes.

A novel type of thioredoxin dedicated to symbiosis in legumes.

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