Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase

Oliver Mueller-Cajar, Mathias Stotz, Petra Wendler, F. Ulrich Hartl, Andreas Bracher () and Manajit Hayer-Hartl ()
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Oliver Mueller-Cajar: Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
Mathias Stotz: Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
Petra Wendler: Gene Center Munich, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25, 81377 Munich, Germany
F. Ulrich Hartl: Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
Andreas Bracher: Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
Manajit Hayer-Hartl: Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany

Nature, 2011, vol. 479, issue 7372, 194-199

Abstract: Abstract Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the fixation of atmospheric CO2 in photosynthesis, but tends to form inactive complexes with its substrate ribulose 1,5-bisphosphate (RuBP). In plants, Rubisco is reactivated by the AAA+ (ATPases associated with various cellular activities) protein Rubisco activase (Rca), but no such protein is known for the Rubisco of red algae. Here we identify the protein CbbX as an activase of red-type Rubisco. The 3.0-Å crystal structure of unassembled CbbX from Rhodobacter sphaeroides revealed an AAA+ protein architecture. Electron microscopy and biochemical analysis showed that ATP and RuBP must bind to convert CbbX into functionally active, hexameric rings. The CbbX ATPase is strongly stimulated by RuBP and Rubisco. Mutational analysis suggests that CbbX functions by transiently pulling the carboxy-terminal peptide of the Rubisco large subunit into the hexamer pore, resulting in the release of the inhibitory RuBP. Understanding Rubisco activation may facilitate efforts to improve CO2 uptake and biomass production by photosynthetic organisms.

Date: 2011
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DOI: 10.1038/nature10568

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