ArticlePhotosynthesis research2006
The diversity and complexity of the cyanobacterial thioredoxin systems.
Article in Photosynthesis research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 77 citations in OpenAlex.
- Thioredoxin A regulates protein synthesis to maintain carbon and nitrogen partitioning in cyanobacteria.Plant physiology · 2024Article
- SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features.Nature communications · 2023Article
- MarineMicrobiology spectrum · 2022Article
- Exploring the Diversity of the Thioredoxin Systems in Cyanobacteria.Antioxidants (Basel, Switzerland) · 2022Review
- Depletion of m-type thioredoxin impairs photosynthesis, carbon fixation, and oxidative stress in cyanobacteria.Plant physiology · 2021Article
- Thioredoxin Dependent Changes in the Redox States of FurA fromAntioxidants (Basel, Switzerland) · 2021Article
- Unexpected diversity of ferredoxin-dependent thioredoxin reductases in cyanobacteria.Plant physiology · 2021Article
- Article
- Recent Advances in the Photoautotrophic Metabolism of Cyanobacteria: Biotechnological Implications.Life (Basel, Switzerland) · 2020Review
- Thioredoxin targets are regulated in heterocysts of cyanobacterium Anabaena sp. PCC 7120 in a light-independent manner.Journal of experimental botany · 2020Article
- Direct Electron Transfer between theApplied and environmental microbiology · 2020Article
- Characterization of TrxC, an Atypical Thioredoxin Exclusively Present in Cyanobacteria.Antioxidants (Basel, Switzerland) · 2018Article
- Structural and functional insights into the unique CBS-CP12 fusion protein family in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural rearrangements in the C-terminal domain homolog of Orange Carotenoid Protein are crucial for carotenoid transfer.Communications biology · 2018Article
- Identifying the Metabolic Differences of a Fast-Growth Phenotype in Synechococcus UTEX 2973.Scientific reports · 2017Article
- NADPH-Thioredoxin Reductase C Mediates the Response to Oxidative Stress and Thermotolerance in the Cyanobacterium Anabaena sp. PCC7120.Frontiers in microbiology · 2016Article
- CopM is a novel copper-binding protein involved in copper resistance in Synechocystis sp. PCC 6803.MicrobiologyOpen · 2015Article
- Responses to oxidative and heavy metal stresses in cyanobacteria: recent advances.International journal of molecular sciences · 2014Review
- Unraveling the redox properties of the global regulator FurA from Anabaena sp. PCC 7120: disulfide reductase activity based on its CXXC motifs.Antioxidants & redox signaling · 2014Article
- Ferredoxin:thioredoxin reductase (FTR) links the regulation of oxygenic photosynthesis to deeply rooted bacteria.Planta · 2013Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cyanobacteria perform oxygenic photosynthesis, which makes them unique among the prokaryotes, and this feature together with their abundance and worldwide distribution renders them a central ecological role. Cyanobacteria and chloroplasts of plants and algae are believed to share a common ancestor and the modern chloroplast would thus be the remnant of an endosymbiosis between a eukaryotic cell and an ancestral oxygenic photosynthetic prokaryote. Chloroplast metabolic processes are coordinated with those of the other cellular compartments and are strictly controlled by means of regulatory systems that commonly involve redox reactions. Disulphide/dithiol exchange catalysed by thioredoxin is a fundamental example of such regulation and represents the molecular mechanism for light-dependent redox control of an ever-increasing number of chloroplast enzymatic activities. In contrast to chloroplast thioredoxins, the functions of the cyanobacterial thioredoxins have long remained elusive, despite their common origin. The sequenced genomes of several cyanobacterial species together with novel experimental approaches involving proteomics have provided new tools for re-examining the roles of the thioredoxin systems in these organisms. Thus, each cyanobacterial genome encodes between one and eight thioredoxins and all components necessary for the reduction of thioredoxins. Screening for thioredoxin target proteins in cyanobacteria indicates that assimilation and storage of nutrients, as well as some central metabolic pathways, are regulated by mechanisms involving disulphide/dithiol exchange, which could be catalysed by thioredoxins or related thiol-containing proteins.
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