An improved Escherichia coli screen for Rubisco identifies a protein-protein interface that can enhance CO₂-fixation kinetics.

ABSTRACT: An overarching goal of photosynthesis research is to identify how components of the process can be improved to benefit crop productivity, global food security, and renewable energy storage. Improving carbon fixation has mostly focused on enhancing the CO₂ fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). This grand challenge has mostly proved ineffective because of catalytic mechanism constraints and required chaperone complementarity that hinder Rubisco biogenesis in alternative hosts. Here we refashion Escherichia coli metabolism by expressing a phosphoribulokinase-neomycin phosphotransferase fusion protein to produce a high-fidelity, high-throughput Rubisco-directed evolution (RDE2) screen that negates false-positive selection. Successive evoluti

SUBMITTER: Wilson RH 

PROVIDER: S-EPMC5766918 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature