Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling

Kazi Waheeda; Heidi Kitchel; Quan Wang; Po Lin Chiu

doi:10.3389/fmolb.2023.1125922

Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling

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

Molecular Sciences, School of (SMS)

Research output: Contribution to journal › Short survey › peer-review

4 Scopus citations

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)
Article number	1125922
Journal	Frontiers in Molecular Biosciences
Volume	10
DOIs	https://doi.org/10.3389/fmolb.2023.1125922
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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10.3389/fmolb.2023.1125922

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title = "Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling",

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.",

keywords = "AAA+ ATPase, Rubisco, Rubisco activase, carbon fixation, photosynthesis, redox",

author = "Kazi Waheeda and Heidi Kitchel and Quan Wang and Chiu, {Po Lin}",

note = "Publisher Copyright: Copyright {\textcopyright} 2023 Waheeda, Kitchel, Wang and Chiu.",

year = "2023",

month = feb,

day = "10",

doi = "10.3389/fmolb.2023.1125922",

language = "English (US)",

volume = "10",

journal = "Frontiers in Molecular Biosciences",

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TY - JOUR

T1 - Molecular mechanism of Rubisco activase

T2 - Dynamic assembly and Rubisco remodeling

AU - Waheeda, Kazi

AU - Kitchel, Heidi

AU - Wang, Quan

AU - Chiu, Po Lin

PY - 2023/2/10

Y1 - 2023/2/10

N2 - 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.

AB - 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.

KW - AAA+ ATPase

KW - Rubisco

KW - Rubisco activase

KW - carbon fixation

KW - photosynthesis

KW - redox

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U2 - 10.3389/fmolb.2023.1125922

DO - 10.3389/fmolb.2023.1125922

M3 - Short survey

AN - SCOPUS:85148767285

SN - 2296-889X

VL - 10

JO - Frontiers in Molecular Biosciences

JF - Frontiers in Molecular Biosciences

M1 - 1125922

ER -

Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling

Abstract

Keywords

ASJC Scopus subject areas

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