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.
Original language | English (US) |
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Article number | 1125922 |
Journal | Frontiers in Molecular Biosciences |
Volume | 10 |
DOIs | |
State | Published - Feb 10 2023 |
Keywords
- AAA+ ATPase
- Rubisco
- Rubisco activase
- carbon fixation
- photosynthesis
- redox
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology (miscellaneous)
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Arizona State University Researchers Update Current Data on Molecular Bioscience (Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling)
2/27/23
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