ArticleThe Journal of biological chemistry2012
Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 66 citations in OpenAlex.
- Hidden protein disorder: Deciphering the structural organisation and dynamics of a non-canonical CP12 from the diatom Thalassiosira pseudonana.The FEBS journal · 2025Article
- 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
- Conformational Disorder Analysis of the Conditionally Disordered Protein CP12 fromInternational journal of molecular sciences · 2023Article
- Exploring the Diversity of the Thioredoxin Systems in Cyanobacteria.Antioxidants (Basel, Switzerland) · 2022Review
- Genome-wide association study and transcriptome analysis dissect the genetic control of silique length in Brassica napus L.Biotechnology for biofuels · 2021Article
- Tyr-Asp inhibition of glyceraldehyde 3-phosphate dehydrogenase affects plant redox metabolism.The EMBO journal · 2021Article
- Flexibility of Oxidized and Reduced States of the Chloroplast Regulatory Protein CP12 in Isolation and in Cell Extracts.Biomolecules · 2021Article
- A new type of flexible CP12 protein in the marine diatom Thalassiosira pseudonana.Cell communication and signaling : CCS · 2021Article
- 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
- 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
- Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii.Scientific reports · 2018Article
- Structural disorder in plant proteins: where plasticity meets sessility.Cellular and molecular life sciences : CMLS · 2017Review
- Didehydrophenylalanine, an abundant modification in the beta subunit of plant polygalacturonases.PloS one · 2017Article
- Comparative cell-specific transcriptomics reveals differentiation of C4 photosynthesis pathways in switchgrass and other C4 lineages.Journal of experimental botany · 2016Article
- Fairy "tails": flexibility and function of intrinsically disordered extensions in the photosynthetic world.Frontiers in molecular biosciences · 2015Review
- Exploring intrinsically disordered proteins using site-directed spin labeling electron paramagnetic resonance spectroscopy.Frontiers in molecular biosciences · 2015Review
- Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs).Chemical reviews · 2014Review
- Review
- The hypervariable amino-terminus of P1 protease modulates potyviral replication and host defense responses.PLoS pathogens · 2014Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Carbon assimilation in plants is regulated by the reduction of specific protein disulfides by light and their re-oxidation in the dark. The redox switch CP12 is an intrinsically disordered protein that can form two disulfide bridges. In the dark oxidized CP12 forms an inactive supramolecular complex with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase, two enzymes of the carbon assimilation cycle. Here we show that binding of CP12 to GAPDH, the first step of ternary complex formation, follows an integrated mechanism that combines conformational selection with induced folding steps. Initially, a CP12 conformation characterized by a circular structural motif including the C-terminal disulfide is selected by GAPDH. Subsequently, the induced folding of the flexible C-terminal tail of CP12 in the active site of GAPDH stabilizes the binary complex. Formation of several hydrogen bonds compensates the entropic cost of CP12 fixation and terminates the interaction mechanism that contributes to carbon assimilation control.
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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.