Frontiers in Molecular Biosciences (Feb 2023)

Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling

  • Kazi Waheeda,
  • Kazi Waheeda,
  • Heidi Kitchel,
  • Heidi Kitchel,
  • Quan Wang,
  • Po-Lin Chiu,
  • Po-Lin Chiu

DOI
https://doi.org/10.3389/fmolb.2023.1125922
Journal volume & issue
Vol. 10

Abstract

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Ribulose-1,5-bisphosphate (RuBP) carboxylase-oxygenase (Rubisco) enzyme is the limiting step of photosynthetic carbon fixation, and its activation is regulated by its co-evolved chaperone, Rubisco activase (Rca). Rca removes the intrinsic sugar phosphate inhibitors occupying the Rubisco active site, allowing RuBP to split into two 3-phosphoglycerate (3PGA) molecules. This review summarizes the evolution, structure, and function of Rca and describes the recent findings regarding the mechanistic model of Rubisco activation by Rca. New knowledge in these areas can significantly enhance crop engineering techniques used to improve crop productivity.

Keywords