Role of small subunit in mediating assembly of red-type form I rubisco

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 th...

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Main Authors: Joshi, Jidnyasa, Mueller-Cajar, Oliver, Tsai, Yi-Chin C., Hartl, F. Ulrich, Hayer-Hartl, Manajit
Other Authors: School of Biological Sciences
Format: Journal Article
Language:English
Published: 2015
Subjects:
Online Access:https://hdl.handle.net/10356/106730
http://hdl.handle.net/10220/25094
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author Joshi, Jidnyasa
Mueller-Cajar, Oliver
Tsai, Yi-Chin C.
Hartl, F. Ulrich
Hayer-Hartl, Manajit
author2 School of Biological Sciences
author_facet School of Biological Sciences
Joshi, Jidnyasa
Mueller-Cajar, Oliver
Tsai, Yi-Chin C.
Hartl, F. Ulrich
Hayer-Hartl, Manajit
author_sort Joshi, Jidnyasa
collection NTU
description 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 β-hairpin extension of red-type RbcS, which is absent in green-type RbcS, is critical for efficient assembly. The β-hairpins of four RbcS subunits form an eight-stranded β-barrel that protrudes into the central solvent channel of the RbcL core complex. The two β-barrels stabilize the complex through multiple interactions with the RbcL subunits. A chimeric green-type RbcS carrying the C-terminal β-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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spelling ntu-10356/1067302023-02-28T17:05:41Z Role of small subunit in mediating assembly of red-type form I rubisco Joshi, Jidnyasa Mueller-Cajar, Oliver Tsai, Yi-Chin C. Hartl, F. Ulrich Hayer-Hartl, Manajit School of Biological Sciences DRNTU::Science::Biological sciences::Biochemistry 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 β-hairpin extension of red-type RbcS, which is absent in green-type RbcS, is critical for efficient assembly. The β-hairpins of four RbcS subunits form an eight-stranded β-barrel that protrudes into the central solvent channel of the RbcL core complex. The two β-barrels stabilize the complex through multiple interactions with the RbcL subunits. A chimeric green-type RbcS carrying the C-terminal β-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. Accepted version 2015-02-25T09:16:46Z 2019-12-06T22:17:07Z 2015-02-25T09:16:46Z 2019-12-06T22:17:07Z 2015 2015 Journal Article 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. 0021-9258 https://hdl.handle.net/10356/106730 http://hdl.handle.net/10220/25094 10.1074/jbc.M114.613091 25371207 en The journal of biological chemistry © 2015 American Society for Biochemistry and Molecular Biology. This is the author created version of a work that has been peer reviewed and accepted for publication by The Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1074/jbc.M114.613091]. 21 p. application/pdf
spellingShingle DRNTU::Science::Biological sciences::Biochemistry
Joshi, Jidnyasa
Mueller-Cajar, Oliver
Tsai, Yi-Chin C.
Hartl, F. Ulrich
Hayer-Hartl, Manajit
Role of small subunit in mediating assembly of red-type form I rubisco
title Role of small subunit in mediating assembly of red-type form I rubisco
title_full Role of small subunit in mediating assembly of red-type form I rubisco
title_fullStr Role of small subunit in mediating assembly of red-type form I rubisco
title_full_unstemmed Role of small subunit in mediating assembly of red-type form I rubisco
title_short Role of small subunit in mediating assembly of red-type form I rubisco
title_sort role of small subunit in mediating assembly of red type form i rubisco
topic DRNTU::Science::Biological sciences::Biochemistry
url https://hdl.handle.net/10356/106730
http://hdl.handle.net/10220/25094
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