Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling

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,...

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Autores principales: Waheeda, Kazi, Kitchel, Heidi, Wang, Quan, Chiu, Po-Lin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Molecular Biosciences
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9951593/
https://www.ncbi.nlm.nih.gov/pubmed/36845545
http://dx.doi.org/10.3389/fmolb.2023.1125922
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author Waheeda, Kazi
Kitchel, Heidi
Wang, Quan
Chiu, Po-Lin
author_facet Waheeda, Kazi
Kitchel, Heidi
Wang, Quan
Chiu, Po-Lin
author_sort Waheeda, Kazi
collection PubMed
description 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.
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spelling pubmed-99515932023-02-25 Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling Waheeda, Kazi Kitchel, Heidi Wang, Quan Chiu, Po-Lin Front Mol Biosci Molecular Biosciences 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. Frontiers Media S.A. 2023-02-10 /pmc/articles/PMC9951593/ /pubmed/36845545 http://dx.doi.org/10.3389/fmolb.2023.1125922 Text en Copyright © 2023 Waheeda, Kitchel, Wang and Chiu. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Molecular Biosciences
Waheeda, Kazi
Kitchel, Heidi
Wang, Quan
Chiu, Po-Lin
Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling
title Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling
title_full Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling
title_fullStr Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling
title_full_unstemmed Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling
title_short Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling
title_sort molecular mechanism of rubisco activase: dynamic assembly and rubisco remodeling
topic Molecular Biosciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9951593/
https://www.ncbi.nlm.nih.gov/pubmed/36845545
http://dx.doi.org/10.3389/fmolb.2023.1125922
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