ArticleThe Journal of biological chemistry2009
CP12 from Chlamydomonas reinhardtii, a permanent specific "chaperone-like" protein of glyceraldehyde-3-phosphate dehydrogenase.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 42 citations in OpenAlex.
- Photosynthetic glyceraldehyde 3-phosphate dehydrogenase B is present in the last common ancestor of Viridiplantae predating the Streptophyta-Chlorophyta split.The New phytologist · 2026Article
- Genome-wide identification and functional characterization of theFrontiers in plant science · 2025Article
- The impact of CP12 on the metabolome of cyanobacteria under fluctuating COFrontiers in plant science · 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
- A Trajectory of Discovery: Metabolic Regulation by the Conditionally Disordered Chloroplast Protein, CP12.Biomolecules · 2022Review
- Reduction in Phosphoribulokinase Amount and Re-Routing Metabolism inInternational journal of molecular sciences · 2022Article
- CP12 Is Involved in Protection against High Light Intensity by Suppressing the ROS Generation inPlants (Basel, Switzerland) · 2021Article
- A new type of flexible CP12 protein in the marine diatom Thalassiosira pseudonana.Cell communication and signaling : CCS · 2021Article
- Article
- Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii.Scientific reports · 2018Article
- Identification of Reference and Biomarker Proteins in Chlamydomonas reinhardtii Cultured under Different Stress Conditions.International journal of molecular sciences · 2017Article
- Arabidopsis CP12 mutants have reduced levels of phosphoribulokinase and impaired function of the Calvin-Benson cycle.Journal of experimental botany · 2017Article
- Cell growth defect factor1/chaperone-like protein of POR1 plays a role in stabilization of light-dependent protochlorophyllide oxidoreductase in Nicotiana benthamiana and Arabidopsis.The Plant cell · 2013Article
- Comparative analysis of 126 cyanobacterial genomes reveals evidence of functional diversity among homologs of the redox-regulated CP12 protein.Plant physiology · 2013Article
- Heme binding properties of glyceraldehyde-3-phosphate dehydrogenase.Biochemistry · 2012Article
- Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly.The Journal of biological chemistry · 2012Article
- DnaJ (Hsp40 protein) binding to folded substrate impacts KplE1 prophage excision efficiency.The Journal of biological chemistry · 2012Article
- An unconventional copper protein required for cytochrome c oxidase respiratory function under extreme acidic conditions.The Journal of biological chemistry · 2010Article
- The chloroplastic thiol reducing systems: dual functions in the regulation of carbohydrate metabolism and regeneration of antioxidant enzymes, emphasis on the poplar redoxin equipment.Photosynthesis research · 2010Review
- Comparative sequence analysis of CP12, a small protein involved in the formation of a Calvin cycle complex in photosynthetic organisms.Photosynthesis research · 2010Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new role is reported for CP12, a highly unfolded and flexible protein, mainly known for its redox function with A(4) glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Both reduced and oxidized CP12 can prevent the in vitro thermal inactivation and aggregation of GAPDH from Chlamydomonas reinhardtii. This mechanism is thus not redox-dependent. The protection is specific to CP12, because other proteins, such as bovine serum albumin, thioredoxin, and a general chaperone, Hsp33, do not fully prevent denaturation of GAPDH. Furthermore, CP12 acts as a specific chaperone, since it does not protect other proteins, such as catalase, alcohol dehydrogenase, or lysozyme. The interaction between CP12 and GAPDH is necessary to prevent the aggregation and inactivation, since the mutant C66S that does not form any complex with GAPDH cannot accomplish this protection. Unlike the C66S mutant, the C23S mutant that lacks the N-terminal bridge is partially able to protect and to slow down the inactivation and aggregation. Tryptic digestion coupled to mass spectrometry confirmed that the S-loop of GAPDH is the interaction site with CP12. Thus, CP12 not only has a redox function but also behaves as a specific "chaperone-like protein" for GAPDH, although a stable and not transitory interaction is observed. This new function of CP12 may explain why it is also present in complexes involving A(2)B(2) GAPDHs that possess a regulatory C-terminal extension (GapB subunit) and therefore do not require CP12 to be redox-regulated.
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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.