Plant RuBisCo assembly in <i>E. coli</i> with five chloroplast chaperones including BSD2.
basic_science · Level V
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- Record sourced from PubMed, PMID 29217567.
- Also identified by DOI 10.1126/science.aap9221.
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Abstract
Plant RuBisCo, a complex of eight large and eight small subunits, catalyzes the fixation of CO<sub>2</sub> in photosynthesis. The low catalytic efficiency of RuBisCo provides strong motivation to reengineer the enzyme with the goal of increasing crop yields. However, genetic manipulation has been hampered by the failure to express plant RuBisCo in a bacterial host. We achieved the functional expression of <i>Arabidopsis thaliana</i> RuBisCo in <i>Escherichia coli</i> by coexpressing multiple chloroplast chaperones. These include the chaperonins Cpn60/Cpn20, RuBisCo accumulation factors 1 and 2, RbcX, and bundle-sheath defective-2 (BSD2). Our structural and functional analysis revealed the role of BSD2 in stabilizing an end-state assembly intermediate of eight RuBisCo large subunits until the small subunits become available. The ability to produce plant RuBisCo recombinantly will facilitate efforts to improve the enzyme through mutagenesis.
Medical subject headings
- Arabidopsis
- Arabidopsis Proteins
- Escherichia coli
- Molecular Chaperones
- Recombinant Proteins
- Ribulose-Bisphosphate Carboxylase