ArticleThe Journal of biological chemistry2013
Small oligomers of ribulose-bisphosphate carboxylase/oxygenase (Rubisco) activase are required for biological activity.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 41 citations in OpenAlex.
- Ribulose-1,5-bisphosphate carboxylase/oxygenase activase isoforms from diverse species show differences in oligomeric structure, thermal stability, and activity.European biophysics journal : EBJ · 2025Article
- Two cowpea Rubisco activase isoforms for crop thermotolerance.The New phytologist · 2025Article
- Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling.Frontiers in molecular biosciences · 2023Review
- A novel chloroplast super-complex consisting of the ATP synthase and photosystem I reaction center.PloS one · 2020Article
- Probing the rice Rubisco-Rubisco activase interaction via subunit heterooligomerization.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Regulation of the leaf proteome by inoculation of Populus × canescens with two Paxillus involutus isolates differing in root colonization rates.Mycorrhiza · 2019Article
- Comparative proteomic study of phytotoxic effects of silver nanoparticles and silver ions on tobacco plants.Environmental science and pollution research international · 2019Article
- Assembly-disassembly is coupled to the ATPase cycle of tobacco Rubisco activase.The Journal of biological chemistry · 2018Article
- The Eukaryotic COCell · 2017Article
- In Vitro Characterization of Thermostable CAM Rubisco Activase Reveals a Rubisco Interacting Surface Loop.Plant physiology · 2017Article
- The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites.Frontiers in molecular biosciences · 2017Review
- Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) activase: product inhibition, cooperativity, and magnesium activation.The Journal of biological chemistry · 2015Article
- Identification of Leaf Proteins Differentially Accumulated between Wheat Cultivars Distinct in Their Levels of Drought Tolerance.PloS one · 2015Article
- Redox regulation of the Calvin-Benson cycle: something old, something new.Frontiers in plant science · 2013Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribulose-bisphosphate carboxylase/oxygenase (Rubisco) activase uses the energy from ATP hydrolysis to remove tight binding inhibitors from Rubisco, thus playing a key role in regulating photosynthesis in plants. Although several structures have recently added much needed structural information for different Rubisco activase enzymes, the arrangement of these subunits in solution remains unclear. In this study, we use a variety of techniques to show that Rubisco activase forms a wide range of structures in solution, ranging from monomers to much higher order species, and that the distribution of these species is highly dependent on protein concentration. The data support a model in which Rubisco activase forms an open spiraling structure rather than a closed hexameric structure. At protein concentrations of 1 μM, corresponding to the maximal activity of the enzyme, Rubisco activase has an oligomeric state of 2-4 subunits. We propose a model in which Rubisco activase requires at least 1 neighboring subunit for hydrolysis of ATP.
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