Exploring the evolutionary protein landscape of Rubisco

During the last decade the practice of laboratory-directed protein evolution has become firmly established as a versatile tool in biochemical research by enabling molecular evolution towards desirable phenotypes or detection of novel structure-function interactions (see Bershtein & Tawfik, 2008, Curr Opin Chem Biol 12: 151-8). Applications of this technique in the field of photosynthesis research have recently been reported in the directed evolution of the CO2-fixing enzyme Rubisco (reviewed by Mueller-Cajar & Whitney, 2008,. Photosyn. Res. 98, 667-75). The goal of increasing photosynthetic efficiency of plants by improving the kinetics of Rubisco has been a long-term goal scoring modest successes.

Projects are available that aim to exploit, and upgrade, our novel Rubisco evolution screening systems to identify mutant Rubisco forms with improved assembly properties and/or enhanced catalytic properties.

Suggested reading

  • Mueller-Cajar O, Whitney SM (2008) Directing the evolution of Rubisco and Rubisco activase: first impressions of a new tool for photosynthesis research. Photosynth Res 98: 667-675