Probing the rice Rubisco–Rubisco activase interaction via subunit heterooligomerization
| Autor: | Devendra Shivhare, Jediael Ng, Oliver Mueller-Cajar, Yi-Chin Candace Tsai |
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| Přispěvatelé: | School of Biological Sciences |
| Rok vydání: | 2019 |
| Předmět: |
Models
Molecular inorganic chemicals Ribulose-Bisphosphate Carboxylase Protein subunit Mutant Random hexamer Photosynthesis Rubisco Activase chemistry.chemical_compound Protein Domains Plant Proteins chemistry.chemical_classification Multidisciplinary Sugar phosphates biology Ribulose fungi RuBisCO Biological sciences [Science] food and beverages Oryza Biological Sciences AAA proteins chemistry Mutagenesis Site-Directed biology.protein Biophysics |
| Zdroj: | Proc Natl Acad Sci U S A |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | 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. Ministry of Education (MOE) Nanyang Technological University This work was funded by a Nanyang Technological University startup grant and Ministry of Education (MOE) of Singapore Tier 2 grant to O.M.-C. (MOE2016-T2-2-088). |
| Databáze: | OpenAIRE |
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