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

Front Mol Biosci. 2023 Feb 10:10:1125922. doi: 10.3389/fmolb.2023.1125922. eCollection 2023.

Authors

Kazi Waheeda^{1

2}, Heidi Kitchel^{1

2}, Quan Wang³, Po-Lin Chiu^{1

2}

Affiliations

¹ School of Molecular Sciences, Arizona State University, Tempe, AZ, United States.
² Biodesign Center for Applied Structural Discovery, Arizona State University, Tempe, AZ, United States.
³ Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, United States.

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.

Publication types

Review

Grants and funding

This work was supported by the U.S. Department of Energy, Office of Science, Basic Energy Sciences (Photosynthetic Systems), under Award Number DE-SC0002423.