ArticlePlant physiology2005
Reconstitution and properties of the recombinant glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase supramolecular complex of Arabidopsis.
Article in Plant physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 81 citations in OpenAlex.
- Genome-wide identification and functional characterization of theFrontiers in plant science · 2025Article
- Post-Translational Modifications to Cysteine Residues in Plant Proteins and Their Impact on the Regulation of Metabolism and Signal Transduction.International journal of molecular sciences · 2024Review
- 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
- A Trajectory of Discovery: Metabolic Regulation by the Conditionally Disordered Chloroplast Protein, CP12.Biomolecules · 2022Review
- The Importance of the C-Terminal Cys Pair of Phosphoribulokinase in Phototrophs in Thioredoxin-Dependent Regulation.Plant & cell physiology · 2022Article
- Proteome-wide identification of S-sulfenylated cysteines reveals metabolic response to freezing stress after cold acclimation inFrontiers in plant science · 2022Article
- The Assembly of Super-Complexes in the Plant Chloroplast.Biomolecules · 2021Review
- Flexibility of Oxidized and Reduced States of the Chloroplast Regulatory Protein CP12 in Isolation and in Cell Extracts.Biomolecules · 2021Article
- COG database update: focus on microbial diversity, model organisms, and widespread pathogens.Nucleic acids research · 2021Article
- Photosynthetic Phosphoribulokinase Structures: Enzymatic Mechanisms and the Redox Regulation of the Calvin-Benson-Bassham Cycle.The Plant cell · 2020Article
- Functional Characterization of Alr0765, A Hypothetical Protein fromCurrent genomics · 2020Article
- Integrating transcriptome and metabolome reveals molecular networks involved in genetic and environmental variation in tobacco.DNA research : an international journal for rapid publication of reports on genes and genomes · 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
- Article
- Feeding the world: improving photosynthetic efficiency for sustainable crop production.Journal of experimental botany · 2019Review
- An L,L-diaminopimelate aminotransferase mutation leads to metabolic shifts and growth inhibition in Arabidopsis.Journal of experimental botany · 2018Article
- Structural and functional insights into the unique CBS-CP12 fusion protein family in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Formation and Change of Chloroplast-Located Plant Metabolites in Response to Light Conditions.International journal of molecular sciences · 2018Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calvin cycle enzymes glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase (PRK) form together with the regulatory peptide CP12 a supramolecular complex in Arabidopsis (Arabidopsis thaliana) that could be reconstituted in vitro using purified recombinant proteins. Both enzyme activities were strongly influenced by complex formation, providing an effective means for regulation of the Calvin cycle in vivo. PRK and CP12, but not GapA (A(4) isoform of GAPDH), are redox-sensitive proteins. PRK was reversibly inhibited by oxidation. CP12 has no enzymatic activity, but it changed conformation depending on redox conditions. GapA, a bispecific NAD(P)-dependent dehydrogenase, specifically formed a binary complex with oxidized CP12 when bound to NAD. PRK did not interact with either GapA or CP12 singly, but oxidized PRK could form with GapA/CP12 a stable ternary complex of about 640 kD (GapA/CP12/PRK). Exchanging NADP for NAD, reducing CP12, or reducing PRK were all conditions that prevented formation of the complex. Although GapA activity was little affected by CP12 alone, the NADPH-dependent activity of GapA embedded in the GapA/CP12/PRK complex was 80% inhibited in respect to the free enzyme. The NADH activity was unaffected. Upon binding to GapA/CP12, the activity of oxidized PRK dropped from 25% down to 2% the activity of the free reduced enzyme. The supramolecular complex was dissociated by reduced thioredoxins, NADP, 1,3-bisphosphoglycerate (BPGA), or ATP. The activity of GapA was only partially recovered after complex dissociation by thioredoxins, NADP, or ATP, and full GapA activation required BPGA. NADP, ATP, or BPGA partially activated PRK, but full recovery of PRK activity required thioredoxins. The reversible formation of the GapA/CP12/PRK supramolecular complex provides novel possibilities to finely regulate GapA ("non-regulatory" GAPDH isozyme) and PRK (thioredoxin sensitive) in a coordinated manner.
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