Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling
Kazi Waheeda, Heidi Kitchel, Quan Wang, Po‐Lin Chiu
Abstract
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.
Topics & Concepts
RuBisCOPhotosynthesisCarbon fixationSugar phosphatesBiochemistryRibulosePyruvate carboxylaseBiologyChloroplastChemistryEnzymeComputational biologyGenePhotosynthetic Processes and MechanismsATP Synthase and ATPases ResearchLight effects on plants