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Title: Probing the rice Rubisco-Rubisco activase interaction via subunit heterooligomerization
Authors: Shivhare, Devendra
Ng, Jediael
Tsai, Candace Yi-Chin
Mueller-Cajar, Oliver
Keywords: Science::Biological sciences
Issue Date: 2019
Source: Shivhare, D., Ng, J., Tsai, C. Y. & Mueller-Cajar, O. (2019). Probing the rice Rubisco-Rubisco activase interaction via subunit heterooligomerization. Proceedings of the National Academy of Sciences, 116(48), 24041-24048.
Project: MOE2016-T2-2-088 
Journal: Proceedings of the National Academy of Sciences 
Abstract: During photosynthesis the AAA+ protein and essential molecular chaperone Rubisco activase (Rca) constantly remodels inhibited active sites of the CO₂-fixing enzyme Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase) to release tightly bound sugar phosphates. Higher plant Rca is a crop improvement target, but its mechanism remains poorly understood. Here we used structure-guided mutagenesis to probe the Rubisco-interacting surface of rice Rca. Mutations in Ser-23, Lys-148, and Arg-321 uncoupled adenosine triphosphatase and Rca activity, implicating them in the Rubisco interaction. Mutant doping experiments were used to evaluate a suite of known Rubisco-interacting residues for relative importance in the context of the functional hexamer. Hexamers containing some subunits that lack the Rubisco-interacting N-terminal domain displayed a ∼2-fold increase in Rca function. Overall Rubisco-interacting residues located toward the rim of the hexamer were found to be less critical to Rca function than those positioned toward the axial pore. Rca is a key regulator of the rate-limiting CO₂-fixing reactions of photosynthesis. A detailed functional understanding will assist the ongoing endeavors to enhance crop CO₂ assimilation rate, growth, and yield.
ISSN: 0027-8424
DOI: 10.1073/pnas.1914245116
DOI (Related Dataset): 10.21979/N9/A2BS0X
Rights: © 2019 The Author(s). Published by National Academy of Sciences. All rights reserved.
Fulltext Permission: none
Fulltext Availability: No Fulltext
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