ArticlePhotosynthesis research2006
Evolution of redoxin genes in the green lineage.
Article in Photosynthesis research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 49 citations in OpenAlex.
- Divergent Protein Redox Dynamics and Their Relationship with Electron Transport Efficiency during Photosynthesis Induction.Plant & cell physiology · 2024Article
- Current Insights into the Redox Regulation Network in Plant Chloroplasts.Plant & cell physiology · 2023Review
- Dissipation of the proton electrochemical gradient in chloroplasts promotes the oxidation of ATP synthase by thioredoxin-like proteins.The Journal of biological chemistry · 2022Article
- Analysis of Thioredoxins and Glutaredoxins in Soybean: Evidence of Translational Regulation under Water Restriction.Antioxidants (Basel, Switzerland) · 2022Article
- Topology of the redox network during induction of photosynthesis as revealed by time-resolved proteomics in tobacco.Science advances · 2021Article
- New Light on Chloroplast Redox Regulation: Molecular Mechanism of Protein Thiol Oxidation.Frontiers in plant science · 2019Review
- Redox Regulation of Starch Metabolism.Frontiers in plant science · 2018Article
- Recombinant ACHT1 from Arabidopsis thaliana: crystallization and X-ray crystallographic analysis.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Roles of N-terminal fatty acid acylations in membrane compartment partitioning: Arabidopsis h-type thioredoxins as a case study.The Plant cell · 2013Article
- Identification and characterization of thioredoxin h isoforms differentially expressed in germinating seeds of the model legume Medicago truncatula.Plant physiology · 2011Article
- The conformational stability and biophysical properties of the eukaryotic thioredoxins of Pisum sativum are not family-conserved.PloS one · 2011Article
- Diversity of chemical mechanisms in thioredoxin catalysis revealed by single-molecule force spectroscopy.Nature structural & molecular biology · 2009Article
- The NADPH-dependent thioredoxin system constitutes a functional backup for cytosolic glutathione reductase in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- A novel extended family of stromal thioredoxins.Plant molecular biology · 2009Article
- Chloroplast NADPH-thioredoxin reductase interacts with photoperiodic development in Arabidopsis.Plant physiology · 2009Article
- A novel type of thioredoxin dedicated to symbiosis in legumes.Plant physiology · 2008Article
- Thioredoxins in chloroplasts.Current genetics · 2007Review
- Inactivation of thioredoxin reductases reveals a complex interplay between thioredoxin and glutathione pathways in Arabidopsis development.The Plant cell · 2007Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The availability of the Arabidopsis genome revealed the complexity of the gene families implicated in dithiol disulfide exchanges. Most non-green organisms present less dithiol oxidoreductase genes. The availability of the almost complete genome sequence of rice now allows a systematic search for thioredoxins, glutaredoxins and their reducers. This shows that all redoxin families previously defined for Arabidopsis have members in the rice genome and that all the deduced rice redoxins fall within these families. This establishes that the redoxin classification applies both to dicots and monocots. Nevertheless, within each redoxin type the number of members is not the same in these two higher plants and it is not always possible to define orthologues between rice and Arabidopsis. The sequencing of two unicellular algae (Chlamydomonas and Ostreococcus) genomes are almost finished. This allowed us to follow the origin of the different gene families in the green lineage. It appears that most thioredoxin and glutaredoxin types, their chloroplastic, mitochondrial and cytosolic reducers are always present in these unicellular organisms. Nevertheless, striking differences appear in comparison to higher plant redoxins. Some thioredoxin types are not present in these algal genomes including thioredoxins o, clot and glutaredoxins CCxC. Numerous redoxins, including the cytosolic thioredoxins, do not fit with the corresponding higher plant classification. In addition both algae present a NADPH-dependent thioredoxin reductase with a selenocysteine which is highly similar to the animal thioredoxin reductases, a type of thioredoxin reductase not present in higher plants.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.