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Coupled chaperone action in folding and assembly of hexadecameric Rubisco

机译：十六聚体Rubisco折叠和组装中的偶联分子伴侣作用

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摘要

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.
机译：形式I Rubisco（核糖1,5-二磷酸羧化酶/加氧酶）是八个大（RbcL）和八个小（RbcS）亚基的复合物，催化大气中CO_2在光合作用中的固定。 Rubisco有限的催化效率引发了为提高农业生产率而重新设计酶的广泛努力。为了促进这种努力，我们通过体外重构和冷冻电子显微镜分析了蓝细菌形式的I Rubisco。我们显示由GroEL / GroES伴侣蛋白折叠的RbcL亚基与伴侣蛋白RbcX_2介导的组装紧密结合。 RbcL单体保持部分不稳定并保持对GroEL的高亲和力，直到被RbcX_2捕获为止。正如RbcL_8-（RbcX_2）_8组装中间体的结构所揭示的那样，RbcX_2在稳定作为二聚体的RbcL亚基方面起着重要作用，并促进了RbcL_8核的组装。最后，添加RbcS会导致RbcX_2释放和全酶形成。当折叠紧密结合到组装时，在形成复杂的寡聚结构时可能更通常需要特定的组装伴侣。

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  • 来源
    《Nature》 |2010年第7278期|197-202|共6页
  • 作者

    Cuimin Liu; Anna L. Young; Amanda Starling-Windhof; Andreas Bracher; Sandra Saschenbrecker; Bharathi Vasudeva Rao; Karnam Vasudeva Rao; Otto Beminghausen; Thorsten Mielke; F.Ulrich Hartl; Roland Beckmann; Manajit Hayer-Hartl;

  • 作者单位

    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany;

    Gene Centre and Center for Integrated Protein Science CIPSM, Department of Chemistry and Biochemistry, University of Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany;

    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany;

    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany;

    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany;

    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany;

    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany;

    Gene Centre and Center for Integrated Protein Science CIPSM, Department of Chemistry and Biochemistry, University of Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany;

    UltraStructure Network, USN, Max Planck Institute for Molecular Genetics, Ihnestrasse 63-73, 14195 Berlin and Charite - Unversitaetsmedizin Berlin, Institut fuer Medizinische Physik und Biophysik, Ziegelstrasse 5-9,10098 Berlin, Germany;

    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany;

    Gene Centre and Center for Integrated Protein Science CIPSM, Department of Chemistry and Biochemistry, University of Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany;

    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany;

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