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  Role of Small Subunit in Mediating Assembly of Red-type Form I Rubisco

Joshi, J., Mueller-Cajar, O., Tsai, Y.-C.-C., Hartl, F. U., & Hayer-Hartl, M. (2015). Role of Small Subunit in Mediating Assembly of Red-type Form I Rubisco. JOURNAL OF BIOLOGICAL CHEMISTRY, 290(2), 1066-1074. doi:10.1074/jbc.M114.613091.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0025-735B-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0025-B43E-7
Genre: Journal Article

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 Creators:
Joshi, Jidnyasa1, Author              
Mueller-Cajar, Oliver1, Author              
Tsai, Yi-Chin C.1, Author              
Hartl, F. Ulrich1, Author              
Hayer-Hartl, Manajit2, 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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Free keywords: RIBULOSE-BISPHOSPHATE CARBOXYLASE/OXYGENASE; RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE; CRYSTAL-STRUCTURE; HEXADECAMERIC RUBISCO; ESCHERICHIA-COLI; 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE; ARABIDOPSIS-THALIANA; OXYGENASE; PROTEIN; CHAPERONE
 Abstract: Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the key enzyme involved in photosynthetic carbon fixation, converting atmospheric CO2 to organic compounds. Form I Rubisco is a cylindrical complex composed of eight large (RbcL) subunits that are capped by four small subunits (RbcS) at the top and four at the bottom. Form I Rubiscos are phylogenetically divided into green-and red-type. Some red-type enzymes have catalytically superior properties. Thus, understanding their folding and assembly is of considerable biotechnological interest. Folding of the green-type RbcL subunits in cyanobacteria is mediated by the GroEL/ES chaperonin system, and assembly to holoenzyme requires specialized chaperones such as RbcX and RAF1. Here, we show that the red-type RbcL subunits in the proteobacterium Rhodobacter sphaeroides also fold with GroEL/ES. However, assembly proceeds in a chaperone-independent manner. We find that the C-terminal beta-hairpin extension of red-type RbcS, which is absent in green-type RbcS, is critical for efficient assembly. The beta-hairpins of four RbcS subunits form an eight-stranded beta-barrel that protrudes into the central solvent channel of the RbcL core complex. The two beta-barrels stabilize the complex through multiple interactions with the RbcL subunits. A chimeric green-type RbcS carrying the C-terminal beta-hairpin renders the assembly of a cyanobacterial Rubisco independent of RbcX. Our results may facilitate the engineering of crop plants with improved growth properties expressing red-type Rubisco.

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Language(s): eng - English
 Dates: 2014-11-042015
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000347778200038
DOI: 10.1074/jbc.M114.613091
 Degree: -

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Title: JOURNAL OF BIOLOGICAL CHEMISTRY
Source Genre: Journal
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Publ. Info: 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Pages: - Volume / Issue: 290 (2) Sequence Number: - Start / End Page: 1066 - 1074 Identifier: ISSN: 0021-9258