ArticleMolecular & cellular proteomics : MCP2014
Proteome-wide light/dark modulation of thiol oxidation in cyanobacteria revealed by quantitative site-specific redox proteomics.
Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed.
- Rapid Adaptation of Cyanobacteria to Environmental Perturbations Is Achieved Through Structural Remodeling of the Proteome.Molecular & cellular proteomics : MCP · 2026Article
- Systematic determination of disulfide bond reduction potentials reveals a nonequilibrium redox hierarchy in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Thiol post-translational modifications modulate allosteric regulation of the OpcA-G6PDH complex through conformational gate control.Protein science : a publication of the Protein Society · 2026Article
- From photosynthetic electron flow to gene regulation: redox signal transduction in cyanobacteria.FEMS microbiology reviews · 2026Review
- Proteome-wide characterization of PTMs reveals host cell responses to viral infection and identifies putative antiviral drug targets.Frontiers in immunology · 2025Review
- Lighting the way: Compelling open questions in photosynthesis research.The Plant cell · 2024Article
- Thioredoxin A regulates protein synthesis to maintain carbon and nitrogen partitioning in cyanobacteria.Plant physiology · 2024Article
- Article
- PTM-Psi: A python package to facilitate the computational investigation of post-translational modification on protein structures and their impacts on dynamics and functions.Protein science : a publication of the Protein Society · 2023Article
- Harnessing redox proteomics to study metabolic regulation and stress response in lignin-fed Rhodococci.Biotechnology for biofuels and bioproducts · 2023Article
- 50 shades of oxidative stress: A state-specific cysteine redox pattern hypothesis.Redox biology · 2023Article
- Circadian regulation of metabolism across photosynthetic organisms.The Plant journal : for cell and molecular biology · 2023Review
- Metabolite interactions in the bacterial Calvin cycle and implications for flux regulation.Communications biology · 2023Article
- Thiol redox proteomics: Characterization of thiol-based post-translational modifications.Proteomics · 2023Review
- Towards the rate limit of heterologous biotechnological reactions in recombinant cyanobacteria.Biotechnology for biofuels and bioproducts · 2023Article
- Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches.Antioxidants (Basel, Switzerland) · 2022Review
- Zam Is a Redox-Regulated Member of the RNB-Family Required for Optimal Photosynthesis in Cyanobacteria.Microorganisms · 2022Article
- Rubredoxin 1 Is Required for Formation of the Functional Photosystem II Core Complex inFrontiers in plant science · 2022Article
- Depletion of m-type thioredoxin impairs photosynthesis, carbon fixation, and oxidative stress in cyanobacteria.Plant physiology · 2021Article
- Redox proteomic study of Bacillus cereus thiol proteome during fermentative anaerobic growth.BMC genomics · 2021Article
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12 authors.
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Abstract
Reversible protein thiol oxidation is an essential regulatory mechanism of photosynthesis, metabolism, and gene expression in photosynthetic organisms. Herein, we present proteome-wide quantitative and site-specific profiling of in vivo thiol oxidation modulated by light/dark in the cyanobacterium Synechocystis sp. PCC 6803, an oxygenic photosynthetic prokaryote, using a resin-assisted thiol enrichment approach. Our proteomic approach integrates resin-assisted enrichment with isobaric tandem mass tag labeling to enable site-specific and quantitative measurements of reversibly oxidized thiols. The redox dynamics of ∼2,100 Cys-sites from 1,060 proteins under light, dark, and 3-(3,4-dichlorophenyl)-1,1-dimethylurea (a photosystem II inhibitor) conditions were quantified. In addition to relative quantification, the stoichiometry or percentage of oxidation (reversibly oxidized/total thiols) for ∼1,350 Cys-sites was also quantified. The overall results revealed broad changes in thiol oxidation in many key biological processes, including photosynthetic electron transport, carbon fixation, and glycolysis. Moreover, the redox sensitivity along with the stoichiometric data enabled prediction of potential functional Cys-sites for proteins of interest. The functional significance of redox-sensitive Cys-sites in NADP-dependent glyceraldehyde-3-phosphate dehydrogenase, peroxiredoxin (AhpC/TSA family protein Sll1621), and glucose 6-phosphate dehydrogenase was further confirmed with site-specific mutagenesis and biochemical studies. Together, our findings provide significant insights into the broad redox regulation of photosynthetic organisms.
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