ArticlePlant physiology1997
The Two Forms of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Activase Differ in Sensitivity to Elevated Temperature.
Article in Plant physiology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 143 citations in OpenAlex.
- Phylogenetic diversity of light-dependent phosphorylation of Thr78 in Rubisco activase.Journal of experimental botany · 2025Article
- 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
- C4 grasses employ distinct strategies to acclimate rubisco activase to heat stress.Bioscience reports · 2024Article
- Transgenic strategies to improve the thermotolerance of photosynthesis.Photosynthesis research · 2023Review
- Short- and long-term warming events on photosynthetic physiology, growth, and yields of field grown crops.The Biochemical journal · 2023Review
- Light Drives and Temperature Modulates: Variation of Phenolic Compounds Profile in Relation to Photosynthesis in Spring Barley.International journal of molecular sciences · 2023Article
- Temperature-induced changes in Arabidopsis Rubisco activity and isoform expression.Journal of experimental botany · 2023Article
- Relevance and Regulation of Alternative Splicing in Plant Heat Stress Response: Current Understanding and Future Directions.Frontiers in plant science · 2022Review
- Enhancing crop yield by using Rubisco activase to improve photosynthesis under elevated temperatures.Stress biology · 2021Review
- The effect of increasing temperature on crop photosynthesis: from enzymes to ecosystems.Journal of experimental botany · 2021Review
- Arabidopsis Plant Natriuretic Peptide Is a Novel Interactor of Rubisco Activase.Life (Basel, Switzerland) · 2020Article
- Mechanisms Regulating the Dynamics of Photosynthesis Under Abiotic Stresses.Frontiers in plant science · 2020Review
- Probing the rice Rubisco-Rubisco activase interaction via subunit heterooligomerization.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Dynamics of Plant Metabolism during Cold Acclimation.International journal of molecular sciences · 2019Review
- HPlants (Basel, Switzerland) · 2019Article
- A Conserved Sequence from Heat-Adapted Species Improves Rubisco Activase Thermostability in Wheat.Plant physiology · 2019Article
- In Vitro Characterization of Thermostable CAM Rubisco Activase Reveals a Rubisco Interacting Surface Loop.Plant physiology · 2017Article
- Transcriptomics Analyses Reveal Wheat Responses to Drought Stress during Reproductive Stages under Field Conditions.Frontiers in plant science · 2017Article
- Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) activase: product inhibition, cooperativity, and magnesium activation.The Journal of biological chemistry · 2015Article
- Fairy "tails": flexibility and function of intrinsically disordered extensions in the photosynthetic world.Frontiers in molecular biosciences · 2015Review
Corrections and comments
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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
Ribulose-1,5-bisphosphate carboxylase/oxygenase activase often consists of two polypeptides that arise from alternative splicing of pre-mRNA. In this study recombinant versions of the spinach (Spinacea oleracea L.) 45- and 41-kD forms of activase were analyzed for their response to temperature. The temperature optimum for ATP hydrolysis by the 45-kD form was 45[deg]C, approximately 13[deg]C higher than the 41-kD form. When the two forms were mixed, the temperature response of the hybrid enzyme was similar to the 45-kD form. In the absence of adenine nucleotide, preincubation of either activase form at temperatures above 25[deg}C inactivated ATPase activity. Adenosine 5[prime]-([gamma]-thio)triphosphate, but not ADP, significantly enhanced the thermostability of the 45-kD form but was much less effective for the 41-kD form. Intrinsic fluorescence showed that the adenosine 5[prime]-([gamma]-thio)triphosphate-induced subunit aggregation was lost at a much lower temperature for the 41-kD than for the 45-kD form. However, the two activase forms were equally susceptible to limited proteolysis after heat treatment. The results indicate that (a) the 45-kD form is more thermostable than, and confers increased thermal stability to, the 41-kD form, and (b) a loss of subunit interactions, rather than enzyme denaturation, appears to be the initial cause of temperature inactivation of activase.
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Registered trials
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