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Improved recombinant expression and purification of functional plant Rubisco

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Wilson,  Robert
Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society;

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Thieulin-Pardo,  Gabriel
Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society;

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Hartl,  Franz-Ulrich
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Hayer-Hartl,  Manajit
Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society;

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Wilson_et_al-2019-FEBS_Letters.pdf
(Publisher version), 529KB

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Citation

Wilson, R., Thieulin-Pardo, G., Hartl, F.-U., & Hayer-Hartl, M. (2019). Improved recombinant expression and purification of functional plant Rubisco. FEBS Letters, 593(6), 611-621. doi:10.1002/1873-3468.13352.


Cite as: http://hdl.handle.net/21.11116/0000-0003-E19E-D
Abstract
Improving the performance of the key photosynthetic enzyme Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) by protein engineering is a critical strategy for increasing crop yields. The extensive chaperone requirement of plant Rubisco for folding and assembly has long been an impediment to this goal. Production of plant Rubisco in Escherichia coli requires the coexpression of the chloroplast chaperonin and four assembly factors. Here, we demonstrate that simultaneous expression of Rubisco and chaperones from a T7 promotor produces high levels of functional enzyme. Expressing the small subunit of Rubisco with a C-terminal hexahistidine-tag further improved assembly, resulting in a similar to 12-fold higher yield than the previously published procedure. The expression system described here provides a platform for the efficient production and engineering of plant Rubisco.