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Structural changes associated with the acute thermal instability of Rubisco activase.
Abstract
Inhibition of photosynthesis by heat has been linked to the instability of the ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) chaperone, Rubisco activase. Examination of the recombinant enzyme showed that ADP and ATP protected against inactivation, whereas Mg(2+) promoted inactivation. Heating caused aggregation of Rubisco activase characterized by disruption of secondary structure content and formation of insoluble protein. In contrast, incubation at room temperature without nucleotide caused the active approximately 660 kDa protein to form a soluble, but inactive aggregate of > 2 x 10(6) Da. Circular dichroism (CD) spectroscopy and fluorescence established that structural perturbations in the aggregate did not reduce alpha-helical content significantly. Differences in the thermal stability between wild type and mutant Rubisco activase were observed for the recombinant proteins and when the proteins were expressed in transgenic Arabidopsis. That the sensitivity of these plants to heat differs indicates that the thermal instability of Rubisco activase is a main determinant of the temperature-sensitivity of photosynthesis.
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The results are consistent with the hypothesis that the intrinsic heat sensitivity of Rubisco activase is linked with the observed decrease in Rubisco activation.
“These results are consistent with the hypothesis that the intrinsic heat sensitivity of Rca is linked with the observed decrease in Rubisco activation (Salvucci and Crafts-Brandner, 2004; Barta et al., 2010; Carmo-Silva and Salvucci, 2011; Scafaro et al., 2016).”
From Rubisco and Rubisco Activase Play an Important Role in the Biochemical Limitations of Photosynthesis in Rice, Wheat, and Maize under High Temperature and Water Deficit (2017) · cites this paper as Barta et al., 2010
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Cited by
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Perdomo, J. A., Capó-Bauçà, S., Carmo-Silva, E., & Galmés, J. (2017) · Frontiers in Plant Science · doi:10.3389/fpls.2017.00490 · Cited by 364
“These results are consistent with the hypothesis that the intrinsic heat sensitivity of Rca is linked with the observed decrease in Rubisco activation (Salvucci and CraftsBrandner, 2004; Barta et al., 2010; Carmo-Silva and Salvucci, 2011; Scafaro et al., 2016).”
Result
Metadata
- Authors
- Barta, C., Dunkle, A. M., Wachter, R. M., & Salvucci, M. E.
- Affiliations
- Agricultural Research Service (US)
- Arizona State University (US)
- Corresponding author
- Salvucci, Michael E.
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 2010-07
- Volume
- 499
- Issue
- 1-2
- Pages
- 17-25
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W2026214597
- Cited by
- 68
- References
- 1
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 1 · 2023: 7 · 2022: 3 · 2021: 8 · 2020: 4 · 2019: 3 · 2018: 2 · 2017: 8 · 2016: 3 · 2015: 2 · 2014: 5 · 2013: 5 · 2012: 7
- FWCI
- 2.21
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- United States Department of Energy, Office of Basic Energy Sciences, Photosynthetic Systems (DE-FG02-08ER20268, DE-PS02-09ER09-02, FG02-09ER16123)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- Rubisco activase, thermal instability, heat-induced protein aggregation, protein denaturation, secondary structure, photosynthesis inhibition, transgenic Arabidopsis, protein mutants, protein thermal stability
- MeSH terms
- Adenosine Diphosphate, Adenosine Triphosphate, Circular Dichroism, Enzyme Activation, Enzyme Stability, Hot Temperature, Magnesium, Photosynthesis, Plant Proteins, Protein Denaturation, Recombinant Proteins, Ribulose-Bisphosphate Carboxylase, Thermodynamics, Arabidopsis, Protein Structure, Secondary, Arabidopsis Proteins, Plants, Genetically Modified, Mutant Proteins, Protein Multimerization
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