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.
Nature – Nature Publishing Group (NPG)
Published: Jan 14, 2010
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