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Journal Article

Complex Chaperone Dependence of Rubisco Biogenesis


Wilson,  Robert H.
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;


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

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Wilson, R. H., & Hayer-Hartl, M. (2018). Complex Chaperone Dependence of Rubisco Biogenesis. Biochemistry, 57(23), 3210-3216. doi:10.1021/acs.biochem.8b00132.

Cite as: https://hdl.handle.net/21.11116/0000-0002-7167-B
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), a similar to 530 kDa complex of 8 large (RbcL) and 8 small subunits (RbcS), mediates the fixation of atmospheric CO2 into usable sugars during photosynthesis. Despite its fundamental role, Rubisco is a remarkably inefficient enzyme and thus is produced by plants in huge amounts. It has long been a key target for bioengineering with the goal to increase crop yields. However, such efforts have been hampered by the complex requirement of Rubisco biogenesis for molecular chaperones. Recent studies have identified an array of auxiliary factors needed for the folding and assembly of the Rubisco subunits. The folding of plant RbcL subunits is mediated by the cylindrical chloroplast chaperonin, Cpn60, and its cofactor Cpn20. Folded RbcL requires a number of additional Rubisco specific assembly chaperones, including RbcX, Rubisco accumulation factors 1 (Raf1) and 2 (Raf2), and the Bundle sheath defective-2 (BSD2), to mediate the assembly of the RbcL, intermediate complex. Incorporation of the RbcS and displacement of the assembly factors generates the active holoenzyme. An Escherichia coli strain expressing the chloroplast chaperonin and auxiliary factors now allows the expression of functional plant Rubisco, paving the way for Rubisco engineering by large scale mutagenesis. Here, we review our current understanding on how these chaperones cooperate to produce one of the most important enzymes in nature.