ArticlePlant physiology2008
A novel type of thioredoxin dedicated to symbiosis in legumes.
Article in Plant physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 72 citations in OpenAlex.
- Article
- Article
- Amino acid motifs for the identification of novel protein interactants.Computational and structural biotechnology journal · 2023Review
- Analysis of Thioredoxins and Glutaredoxins in Soybean: Evidence of Translational Regulation under Water Restriction.Antioxidants (Basel, Switzerland) · 2022Article
- The Nitrate Transporter MtNPF6.8 Is a Master Sensor of Nitrate Signal in the Primary Root Tip ofFrontiers in plant science · 2022Article
- Molecular responses of legumes to abiotic stress: post-translational modifications of proteins and redox signaling.Journal of experimental botany · 2021Review
- Thioredoxin Network in Plant Mitochondria: Cysteine S-Posttranslational Modifications and Stress Conditions.Frontiers in plant science · 2020Review
- Glutathione Deficiency inFrontiers in plant science · 2020Article
- Involvement of Glutaredoxin and Thioredoxin Systems in the Nitrogen-Fixing Symbiosis between Legumes and Rhizobia.Antioxidants (Basel, Switzerland) · 2018Review
- Identification of effector-like proteins in Trichoderma spp. and role of a hydrophobin in the plant-fungus interaction and mycoparasitism.BMC genetics · 2017Article
- Nitric oxide is required for the auxin-induced activation of NADPH-dependent thioredoxin reductase and protein denitrosylation during root growth responses in arabidopsis.Annals of botany · 2015Article
- A novel motif in the NaTrxh N-terminus promotes its secretion, whereas the C-terminus participates in its interaction with S-RNase in vitro.BMC plant biology · 2014Article
- Increasing Phosphatidylinositol (4,5)-Bisphosphate Biosynthesis Affects Basal Signaling and Chloroplast Metabolism in Arabidopsis thaliana.Plants (Basel, Switzerland) · 2014Article
- Thiol-based redox signaling in the nitrogen-fixing symbiosis.Frontiers in plant science · 2013Review
- Transcriptome analysis of resistant soybean roots infected by Meloidogyne javanica.Genetics and molecular biology · 2012Article
- Isolation, identification and sequence analysis of a thioredoxin h gene, a member of subgroup III of h-type Trxs from grape (Vitis vinifera L. cv. Askari).Molecular biology reports · 2012Article
- Role of cysteine residues and disulfide bonds in the activity of a legume root nodule-specific, cysteine-rich peptide.The Journal of biological chemistry · 2012Article
- Peroxiredoxins and NADPH-dependent thioredoxin systems in the model legume Lotus japonicus.Plant physiology · 2011Article
- Identification and characterization of thioredoxin h isoforms differentially expressed in germinating seeds of the model legume Medicago truncatula.Plant physiology · 2011Article
- The chloroplastic thiol reducing systems: dual functions in the regulation of carbohydrate metabolism and regeneration of antioxidant enzymes, emphasis on the poplar redoxin equipment.Photosynthesis research · 2010Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
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