Cited by 68Photosynthetic Processes and MechanismsProtein Structure and DynamicsHeat shock proteins research

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Structural changes associated with the acute thermal instability of Rubisco activase.

Barta, Csengele, Dunkle, Alison M., Wachter, Rebekka M., Salvucci, Michael E.·2010·Archives of Biochemistry and Biophysics

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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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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