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September 12, 2025European Biophysics JournalOpen Access

Ribulose-1,5-bisphosphate carboxylase/oxygenase activase isoforms from diverse species show differences in oligomeric structure, thermal stability, and activity

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Authors

JKJ.R. KeownCentre for Human GeneticsSWSerena A.J. WatkinUniversity of CanterburyFPF. Grant PearceUniversity of Canterbury

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Implication

This study shows differences in oligomeric structure and thermal stability of Rubisco activase isoforms, highlighting their diverse functionalities across species.

Key Points

  • Hexamer-forming isoforms exhibited superior Rubisco reactivation and ATP hydrolysis activities, enhancing photosynthetic efficiency.
  • Cotton and creosote Rca isoforms formed highly polydisperse complexes, lacking discrete hexamer formation even with ATP.
  • Antarctic hairgrass α-Rca and Sitka spruce β-Rca formed stable hexamers under similar conditions, reflecting structural diversity.
  • Thermal stability assays indicated that hexamer formation may enhance stability and activity in select Rca isoforms.

Cite This Study

Keown et al. (2025) studied this question.

synapsesocial.com/papers/68d44a3031b076d99fa533a0https://doi.org/10.1007/s00249-025-01794-4
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Also Consider

Synapse has enriched 2 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Protein stability induced by ligand binding correlates with changes in protein flexibility2003 · 257 citations
  2. 2Nucleotide Dependence of Subunit Rearrangements in Short-Form Rubisco Activase from Spinach2017 · 8 citations