ArticleThe Journal of biological chemistry2014
Thioredoxin-dependent redox regulation of chloroplastic phosphoglycerate kinase from Chlamydomonas reinhardtii.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 45 citations in OpenAlex.
- Reduction in chloroplastic ribulose-5-phosphate-3-epimerase decreases photosynthetic capacity in Arabidopsis.Frontiers in plant science · 2022Article
- Plasticity in plastid redox networks: evolution of glutathione-dependent redox cascades and glutathionylation sites.BMC plant biology · 2021Article
- Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea.Open biology · 2020Review
- Biochemical insight into redox regulation of plastidial 3-phosphoglycerate dehydrogenase fromThe Journal of biological chemistry · 2020Article
- High-Resolution Crystal Structure of Chloroplastic Ribose-5-Phosphate Isomerase fromInternational journal of molecular sciences · 2020Article
- Copper-induced concomitant increases in photosynthesis, respiration, and C, N and S assimilation revealed by transcriptomic analyses in Ulva compressa (Chlorophyta).BMC plant biology · 2020Article
- Article
- Insights into the function of NADPH thioredoxin reductase C (NTRC) based on identification of NTRC-interacting proteins in vivo.Journal of experimental botany · 2019Article
- Article
- Crystal Structure of Chloroplastic Thioredoxin f2 fromAntioxidants (Basel, Switzerland) · 2018Article
- The phosphorylated redox proteome of Chlamydomonas reinhardtii: Revealing novel means for regulation of protein structure and function.Redox biology · 2018Article
- MinOmics, an Integrative and Immersive Tool for Multi-Omics Analysis.Journal of integrative bioinformatics · 2018Article
- Comprehensive Redox Profiling of the Thiol Proteome ofMolecular & cellular proteomics : MCP · 2018Article
- Phosphoglycerate Kinases Are Co-Regulated to Adjust Metabolism and to Optimize Growth.Plant physiology · 2018Article
- Regulation of the Calvin-Benson-Bassham cycle in the enigmatic diatoms: biochemical and evolutionary variations on an original theme.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Calredoxin represents a novel type of calcium-dependent sensor-responder connected to redox regulation in the chloroplast.Nature communications · 2016Article
- Circadian Profiling of the Arabidopsis Proteome Using 2D-DIGE.Frontiers in plant science · 2016Article
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In photosynthetic organisms, thioredoxin-dependent redox regulation is a well established mechanism involved in the control of a large number of cellular processes, including the Calvin-Benson cycle. Indeed, 4 of 11 enzymes of this cycle are activated in the light through dithiol/disulfide interchanges controlled by chloroplastic thioredoxin. Recently, several proteomics-based approaches suggested that not only four but all enzymes of the Calvin-Benson cycle may withstand redox regulation. Here, we characterized the redox features of the Calvin-Benson enzyme phosphoglycerate kinase (PGK1) from the eukaryotic green alga Chlamydomonas reinhardtii, and we show that C. reinhardtii PGK1 (CrPGK1) activity is inhibited by the formation of a single regulatory disulfide bond with a low midpoint redox potential (-335 mV at pH 7.9). CrPGK1 oxidation was found to affect the turnover number without altering the affinity for substrates, whereas the enzyme activation appeared to be specifically controlled by f-type thioredoxin. Using a combination of site-directed mutagenesis, thiol titration, mass spectrometry analyses, and three-dimensional modeling, the regulatory disulfide bond was shown to involve the not strictly conserved Cys(227) and Cys(361). Based on molecular mechanics calculation, the formation of the disulfide is proposed to impose structural constraints in the C-terminal domain of the enzyme that may lower its catalytic efficiency. It is therefore concluded that CrPGK1 might constitute an additional light-modulated Calvin-Benson cycle enzyme with a low activity in the dark and a TRX-dependent activation in the light. These results are also discussed from an evolutionary point of view.
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