ArticleFrontiers in plant science2013
The hydrogen peroxide-sensitive proteome of the chloroplast in vitro and in vivo.
Article in Frontiers in plant science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.
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Who cites it
36 citing papers in PubMed, 1 synthesis or guideline pooled it, 80 citations in OpenAlex.
- Hydrogen Peroxide: Its Role in Plant Biology and Crosstalk with Signalling Networks.International journal of molecular sciences · 2018Pooled it
- Nitrogen Assimilation Plays a Role in Balancing the Chloroplastic Glutathione Redox Potential Under High Light Conditions.Plant, cell & environment · 2025Article
- Divergent Protein Redox Dynamics and Their Relationship with Electron Transport Efficiency during Photosynthesis Induction.Plant & cell physiology · 2024Article
- The ascorbate-glutathione cycle coming of age.Journal of experimental botany · 2024Review
- Methyl viologen-induced changes in the Arabidopsis proteome implicate PATELLIN 4 in oxidative stress responses.Journal of experimental botany · 2024Article
- Redox and Hormonal Changes in the Transcriptome of Grape (Plants (Basel, Switzerland) · 2022Article
- Review
- Article
- Topology of the redox network during induction of photosynthesis as revealed by time-resolved proteomics in tobacco.Science advances · 2021Article
- Measuring ROS and redox markers in plant cells.RSC chemical biology · 2021Review
- The major photoprotective role of anthocyanins in leaves of Arabidopsis thaliana under long-term high light treatment: antioxidant or light attenuator?Photosynthesis research · 2021Article
- Photosynthetic Metabolism and Nitrogen Reshuffling Are Regulated by Reversible Cysteine Thiol Oxidation Following Nitrogen Deprivation in Chlamydomonas.Plants (Basel, Switzerland) · 2020Article
- Chloroplast-associated molecular patterns as concept for fine-tuned operational retrograde signalling.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020Review
- Arabidopsis BSD2 reveals a novel redox regulation of Rubisco physiologyPlant signaling & behavior · 2020Article
- S-Nitroso-Proteome Revealed in Stomatal Guard Cell Response to Flg22.International journal of molecular sciences · 2020Article
- Oxygen and ROS in Photosynthesis.Plants (Basel, Switzerland) · 2020Review
- Inhibition of TOR inCells · 2019Article
- Proteome-Wide Analysis of Cysteine Reactivity during Effector-Triggered Immunity.Plant physiology · 2019Article
- Reactive Oxygen Species and the Redox-Regulatory Network in Cold Stress Acclimation.Antioxidants (Basel, Switzerland) · 2018Review
- Redox regulation of type-I inositol trisphosphate receptors in intact mammalian cells.The Journal of biological chemistry · 2018Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hydrogen peroxide (H2O2) evolves during cellular metabolism and accumulates under various stresses causing serious redox imbalances. Many proteomics studies aiming to identify proteins sensitive to H2O2 used concentrations that were above the physiological range. Here the chloroplast proteins were subjected to partial oxidation by exogenous addition of H2O2 equivalent to 10% of available protein thiols which allowed for the identification of the primary targets of oxidation. The chosen redox proteomic approach employed differential labeling of non-oxidized and oxidized thiols using sequential alkylation with N-ethylmaleimide and biotin maleimide. The in vitro identified proteins are involved in carbohydrate metabolism, photosynthesis, redox homeostasis, and nitrogen assimilation. By using methyl viologen that induces oxidative stress in vivo, mostly the same primary targets of oxidation were identified and several oxidation sites were annotated. Ribulose-1,5-bisphosphate (RubisCO) was a primary oxidation target. Due to its high abundance, RubisCO is suggested to act as a chloroplast redox buffer to maintain a suitable redox state, even in the presence of increased reactive oxygen species release. 2-cysteine peroxiredoxins (2-Cys Prx) undergo redox-dependent modifications and play important roles in antioxidant defense and signaling. The identification of 2-Cys Prx was expected based on its high affinity to H2O2 and is considered as a proof of concept for the approach. Targets of Trx, such as phosphoribulokinase, glyceraldehyde-3-phosphate dehydrogenase, transketolase, and sedoheptulose-1,7-bisphosphatase have at least one regulatory disulfide bridge which supports the conclusion that the identified proteins undergo reversible thiol oxidation. In conclusion, the presented approach enabled the identification of early targets of H2O2 oxidation within the cellular proteome under physiological experimental conditions.
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