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

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

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

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Tsai,  Yi-Chin C.
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Hartl,  F. 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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Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0025-735B-9
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.