ArticleProceedings of the National Academy of Sciences of the United States of America2008
Thioredoxin-mediated reversible dissociation of a stromal multiprotein complex in response to changes in light availability.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
50 citing papers in PubMed, 115 citations in OpenAlex.
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- NTRC regulates CP12 to activate Calvin-Benson cycle during cold acclimation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Glyceraldehyde-3-phosphate dehydrogenase subunits A and B are essential to maintain photosynthetic efficiency.Plant physiology · 2023Article
- Conformational Disorder Analysis of the Conditionally Disordered Protein CP12 fromInternational journal of molecular sciences · 2023Article
- The Importance of the C-Terminal Cys Pair of Phosphoribulokinase in Phototrophs in Thioredoxin-Dependent Regulation.Plant & cell physiology · 2022Article
- Reciprocity between a retrograde signal and a putative metalloprotease reconfigures plastidial metabolic and structural states.Science advances · 2022Article
- Exploring the Diversity of the Thioredoxin Systems in Cyanobacteria.Antioxidants (Basel, Switzerland) · 2022Review
- Topology of the redox network during induction of photosynthesis as revealed by time-resolved proteomics in tobacco.Science advances · 2021Article
- The Assembly of Super-Complexes in the Plant Chloroplast.Biomolecules · 2021Review
- Probing Light-Dependent Regulation of the Calvin Cycle Using a Multi-Omics Approach.Frontiers in plant science · 2021Article
- Molecular Mechanisms Underlying the Acclimation ofFrontiers in plant science · 2021Article
- Dynamic light caused less photosynthetic suppression, rather than more, under nitrogen deficit conditions than under sufficient nitrogen supply conditions in soybean.BMC plant biology · 2020Article
- Redox Conformation-Specific Protein-Protein Interactions of the 2-Cysteine Peroxiredoxin in Arabidopsis.Antioxidants (Basel, Switzerland) · 2020Article
- Proteomic Analysis of Rice Subjected to Low Light Stress and Overexpression of OsGAPB Increases the Stress Tolerance.Rice (New York, N.Y.) · 2020Article
- Photosynthetic Phosphoribulokinase Structures: Enzymatic Mechanisms and the Redox Regulation of the Calvin-Benson-Bassham Cycle.The Plant cell · 2020Article
- Structural basis of light-induced redox regulation in the Calvin-Benson cycle in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Darkness-induced effects on gene expression in Cosmarium crenatum (Zygnematophyceae) from a polar habitat.Scientific reports · 2019Article
- Article
- Crystal structure of phosphoribulokinase from Synechococcus sp. strain PCC 6301.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Feeding the world: improving photosynthetic efficiency for sustainable crop production.Journal of experimental botany · 2019Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
A Calvin cycle multiprotein complex including phosphoribulokinase (PRK), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and a small protein, CP12, has previously been identified. In this article, we have studied this complex in leaves and have shown that dissociation and reassociation of the PRK/GAPDH/CP12 complex occurs in a time frame of minutes, allowing for rapid regulation of enzyme activity. Furthermore, we have shown that the extent of formation and dissociation of the PRK/GAPDH/CP12 complex correlates with the quantity of light. These data provide evidence linking the status of this complex with the rapid and subtle regulation of GAPDH and PRK activities in response to fluctuations in light availability. We have also demonstrated that dissociation of this complex depends on electron transport chain activity and that the major factor involved in the dissociation of the pea complex was thioredoxin f. We show here that both PRK and GAPDH are present in the reduced form in leaves in the dark, but are inactive, demonstrating the role of the PRK/GAPDH/CP12 complex in deactivating these enzymes in response to reductions in light intensity. Based on our data, we propose a model for thioredoxin f-mediated activation of PRK and GAPDH by two mechanisms: directly through reduction of disulfide bonds within these enzymes and indirectly by mediating the breakdown of the complex in response to changes in light intensity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.