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  Plant RuBisCo assembly in E. coli with five chloroplast chaperones including BSD2

Aigner, H., Wilson, R. H., Bracher, A., Calisse, L., Bhat, J. Y., Hartl, F. U., et al. (2017). Plant RuBisCo assembly in E. coli with five chloroplast chaperones including BSD2. Science, 358(6368), 1272-1278. doi:10.1126/science.aap9221.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-8B4D-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-8B4E-9
Genre: Journal Article

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 Creators:
Aigner, H.1, Author              
Wilson, R. H.1, Author              
Bracher, A.1, Author              
Calisse, L.1, Author              
Bhat, J. Y.1, Author              
Hartl, F. U.1, Author              
Hayer-Hartl, M.2, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              

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 Abstract: Plant RuBisCo, a complex of eight large and eight small subunits, catalyzes the fixation of CO2 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 Arabidopsis thaliana RuBisCo in Escherichia coli 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.

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 Dates: 2017-12-08
 Publication Status: Published in print
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 Identifiers: DOI: 10.1126/science.aap9221
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Title: Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 358 (6368) Sequence Number: - Start / End Page: 1272 - 1278 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1