ArticleNature plants2017
Expansion of the redox-sensitive proteome coincides with the plastid endosymbiosis.
Article in Nature plants, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 40 citations in OpenAlex.
- Taming the perils of photosynthesis by eukaryotes: constraints on endosymbiotic evolution in aquatic ecosystems.Communications biology · 2023Review
- Glutathione Metabolism in Plants under Stress: Beyond Reactive Oxygen Species Detoxification.Metabolites · 2021Review
- Plasticity in plastid redox networks: evolution of glutathione-dependent redox cascades and glutathionylation sites.BMC plant biology · 2021Article
- Independent evolution of the thioredoxin system in photosynthetic Paulinella species.Current biology : CB · 2021Article
- The evolutionary conserved iron-sulfur protein TCR controls P700 oxidation in photosystem I.iScience · 2021Article
- Biochemical Characterization of a Novel Redox-Regulated Metacaspase in a Marine Diatom.Frontiers in microbiology · 2021Article
- Retrograde Signaling: Understanding the Communication between Organelles.International journal of molecular sciences · 2020Review
- Horizontal and endosymbiotic gene transfer in early plastid evolution.The New phytologist · 2019Review
- Article
- Reactive oxygen species, oxidative signaling and the regulation of photosynthesis.Environmental and experimental botany · 2018Review
- Photosynthesis solutions to enhance productivity.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Article
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5 authors at 2 institutions in 2 countries.
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Abstract
The redox-sensitive proteome (RSP) consists of protein thiols that undergo redox reactions, playing an important role in coordinating cellular processes. Here, we applied a large-scale phylogenomic reconstruction approach in the model diatom Phaeodactylum tricornutum to map the evolutionary origins of the eukaryotic RSP. The majority of P. tricornutum redox-sensitive cysteines (76%) is specific to eukaryotes, yet these are encoded in genes that are mostly of a prokaryotic origin (57%). Furthermore, we find a threefold enrichment in redox-sensitive cysteines in genes that were gained by endosymbiotic gene transfer during the primary plastid acquisition. The secondary endosymbiosis event coincides with frequent introduction of reactive cysteines into existing proteins. While the plastid acquisition imposed an increase in the production of reactive oxygen species, our results suggest that it was accompanied by significant expansion of the RSP, providing redox regulatory networks the ability to cope with fluctuating environmental conditions.
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