Synthetic Manihot esculenta Rubisco activase proteins with increased thermotolerance identified via machine learning

2025/07/30 by Clayton M. Dilks, Rhiannon J. LaVine, Claire M. Buchanan +2
Agricultural and Biological Sciences · Biochemistry, Genetics and Molecular Biology · #Cassava research and cyanide #Photosynthetic Processes and Mechanisms #Plant Micronutrient Interactions and Effects

paper · doi:10.17912/micropub.biology.001773

openalex publication_date 2025/07/30 · openalex created_date 2025/10/25 · openalex updated_date 2026/07/01

Abstract

Adaptation to increasing environmental temperatures is essential to plant survival and human food production. Thermal tolerance is controlled by a complex network of factors in plants including but not limited to genetic variation and environmental context. Rubisco activase (Rca) is a key photosynthetic enzyme with low thermal tolerance. Here, we report a large machine learning-directed screen of >1,400 synthetic cassava Rca enzymes which identified mutations that convey increased thermal stability while minimizing introduced mutations. We demonstrate multiple synthetic proteins that maintain activity at 8°C higher than wildtype cassava Rca including a single mutation that retains most activity post heat-shock.

Related

• The α form of Rubisco activase supports photosynthesis during heat stress in the absence of the β form in Setaria viridis
• Predicting plant thermal responses using a temperature-aware plant metabolic model: a primer
• Metabolic modeling identifies determinants of thermal growth responses in Arabidopsis thaliana
• Convergence, stability, and thermal adaptation of the rubisco large subunit in plants
• Engineering carbon assimilation in plants