Coupled chaperone action in folding and assembly of hexadecameric Rubisco

Coupled chaperone action in folding and assembly of hexadecameric Rubisco Form I Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase), a complex of eight large (RbcL) and eight small (RbcS) subunits, catalyses the fixation of atmospheric CO 2 in photosynthesis. The limited catalytic efficiency of Rubisco has sparked extensive efforts to re-engineer the enzyme with the goal of enhancing agricultural productivity. To facilitate such efforts we analysed the formation of cyanobacterial form I Rubisco by in vitro reconstitution and cryo-electron microscopy. We show that RbcL subunit folding by the GroEL/GroES chaperonin is tightly coupled with assembly mediated by the chaperone RbcX 2 . RbcL monomers remain partially unstable and retain high affinity for GroEL until captured by RbcX 2 . As revealed by the structure of a RbcL 8 –(RbcX 2 ) 8 assembly intermediate, RbcX 2 acts as a molecular staple in stabilizing the RbcL subunits as dimers and facilitates RbcL 8 core assembly. Finally, addition of RbcS results in RbcX 2 release and holoenzyme formation. Specific assembly chaperones may be required more generally in the formation of complex oligomeric structures when folding is closely coupled to assembly. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Nature Publishing Group (NPG)

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Publisher
Nature Publishing Group (NPG)
Copyright
Copyright © 2010 Macmillan Publishers Limited. All rights reserved
ISSN
0028-0836
eISSN
1476-4687
D.O.I.
10.1038/nature08651
Publisher site
See Article on Publisher Site

Abstract

Form I Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase), a complex of eight large (RbcL) and eight small (RbcS) subunits, catalyses the fixation of atmospheric CO 2 in photosynthesis. The limited catalytic efficiency of Rubisco has sparked extensive efforts to re-engineer the enzyme with the goal of enhancing agricultural productivity. To facilitate such efforts we analysed the formation of cyanobacterial form I Rubisco by in vitro reconstitution and cryo-electron microscopy. We show that RbcL subunit folding by the GroEL/GroES chaperonin is tightly coupled with assembly mediated by the chaperone RbcX 2 . RbcL monomers remain partially unstable and retain high affinity for GroEL until captured by RbcX 2 . As revealed by the structure of a RbcL 8 –(RbcX 2 ) 8 assembly intermediate, RbcX 2 acts as a molecular staple in stabilizing the RbcL subunits as dimers and facilitates RbcL 8 core assembly. Finally, addition of RbcS results in RbcX 2 release and holoenzyme formation. Specific assembly chaperones may be required more generally in the formation of complex oligomeric structures when folding is closely coupled to assembly.

Journal

NatureNature Publishing Group (NPG)

Published: Jan 14, 2010

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