Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling.
AAA+ ATPase
Rubisco
Rubisco activase
carbon fixation
photosynthesis
redox
Journal
Frontiers in molecular biosciences
ISSN: 2296-889X
Titre abrégé: Front Mol Biosci
Pays: Switzerland
ID NLM: 101653173
Informations de publication
Date de publication:
2023
2023
Historique:
received:
16
12
2022
accepted:
31
01
2023
entrez:
27
2
2023
pubmed:
28
2
2023
medline:
28
2
2023
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 36845545
doi: 10.3389/fmolb.2023.1125922
pii: 1125922
pmc: PMC9951593
doi:
Types de publication
Journal Article
Review
Langues
eng
Pagination
1125922Informations de copyright
Copyright © 2023 Waheeda, Kitchel, Wang and Chiu.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. The reviewer HL declared a past co-authorship with one of the authors P-LC to the handling Editor.
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