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Coupled chaperone action in folding and assembly of hexadecameric Rubisco

Author

Listed:
  • Cuimin Liu

    (Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany)

  • Anna L. Young

    (Gene Centre and Center for Integrated Protein Science CIPSM, University of Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany)

  • Amanda Starling-Windhof

    (Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany)

  • Andreas Bracher

    (Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany)

  • Sandra Saschenbrecker

    (Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany)

  • Bharathi Vasudeva Rao

    (Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany)

  • Karnam Vasudeva Rao

    (Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany)

  • Otto Berninghausen

    (Gene Centre and Center for Integrated Protein Science CIPSM, University of Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany)

  • Thorsten Mielke

    (UltraStructure Network, USN, Max Planck Institute for Molecular Genetics, Ihnestrasse 63–73, 14195 Berlin and Charité – Unversitätsmedizin Berlin, Institut für Medizinische Physik und Biophysik, Ziegelstraße 5–9, 10098 Berlin, Germany)

  • F. Ulrich Hartl

    (Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany)

  • Roland Beckmann

    (Gene Centre and Center for Integrated Protein Science CIPSM, University of Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany)

  • Manajit Hayer-Hartl

    (Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany)

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 CO2 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 RbcX2. RbcL monomers remain partially unstable and retain high affinity for GroEL until captured by RbcX2. As revealed by the structure of a RbcL8–(RbcX2)8 assembly intermediate, RbcX2 acts as a molecular staple in stabilizing the RbcL subunits as dimers and facilitates RbcL8 core assembly. Finally, addition of RbcS results in RbcX2 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.

Suggested Citation

  • Cuimin Liu & Anna L. Young & Amanda Starling-Windhof & Andreas Bracher & Sandra Saschenbrecker & Bharathi Vasudeva Rao & Karnam Vasudeva Rao & Otto Berninghausen & Thorsten Mielke & F. Ulrich Hartl & , 2010. "Coupled chaperone action in folding and assembly of hexadecameric Rubisco," Nature, Nature, vol. 463(7278), pages 197-202, January.
    • Handle: RePEc:nat:nature:v:463:y:2010:i:7278:d:10.1038_nature08651
    DOI: 10.1038/nature08651
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