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Rubisco forms a lattice inside alpha-carboxysomes

Author

Listed:
  • Lauren Ann Metskas

    (California Institute of Technology
    Purdue University
    Purdue University)

  • Davi Ortega

    (California Institute of Technology)

  • Luke M. Oltrogge

    (University of California)

  • Cecilia Blikstad

    (University of California
    Ångström Laboratory, Uppsala University)

  • Derik R. Lovejoy

    (Purdue University)

  • Thomas G. Laughlin

    (University of California
    University of California)

  • David F. Savage

    (University of California)

  • Grant J. Jensen

    (California Institute of Technology
    Brigham Young University)

Abstract

Despite the importance of microcompartments in prokaryotic biology and bioengineering, structural heterogeneity has prevented a complete understanding of their architecture, ultrastructure, and spatial organization. Here, we employ cryo-electron tomography to image α-carboxysomes, a pseudo-icosahedral microcompartment responsible for carbon fixation. We have solved a high-resolution subtomogram average of the Rubisco cargo inside the carboxysome, and determined the arrangement of the enzyme. We find that the H. neapolitanus Rubisco polymerizes in vivo, mediated by the small Rubisco subunit. These fibrils can further pack to form a lattice with six-fold pseudo-symmetry. This arrangement preserves freedom of motion and accessibility around the Rubisco active site and the binding sites for two other carboxysome proteins, CsoSCA (a carbonic anhydrase) and the disordered CsoS2, even at Rubisco concentrations exceeding 800 μM. This characterization of Rubisco cargo inside the α-carboxysome provides insight into the balance between order and disorder in microcompartment organization.

Suggested Citation

  • Lauren Ann Metskas & Davi Ortega & Luke M. Oltrogge & Cecilia Blikstad & Derik R. Lovejoy & Thomas G. Laughlin & David F. Savage & Grant J. Jensen, 2022. "Rubisco forms a lattice inside alpha-carboxysomes," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32584-7
    DOI: 10.1038/s41467-022-32584-7
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    References listed on IDEAS

    as
    1. Hector Garcia-Seisdedos & Charly Empereur-Mot & Nadav Elad & Emmanuel D. Levy, 2017. "Proteins evolve on the edge of supramolecular self-assembly," Nature, Nature, vol. 548(7666), pages 244-247, August.
    2. H. Wang & X. Yan & H. Aigner & A. Bracher & N. D. Nguyen & W. Y. Hee & B. M. Long & G. D. Price & F. U. Hartl & M. Hayer-Hartl, 2019. "Rubisco condensate formation by CcmM in β-carboxysome biogenesis," Nature, Nature, vol. 566(7742), pages 131-135, February.
    3. Tao Ni & Yaqi Sun & Will Burn & Monsour M. J. Al-Hazeem & Yanan Zhu & Xiulian Yu & Lu-Ning Liu & Peijun Zhang, 2022. "Structure and assembly of cargo Rubisco in two native α-carboxysomes," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
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    Cited by:

    1. Guole Liu & Tongxin Niu & Mengxuan Qiu & Yun Zhu & Fei Sun & Ge Yang, 2024. "DeepETPicker: Fast and accurate 3D particle picking for cryo-electron tomography using weakly supervised deep learning," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Taiyu Chen & Marta Hojka & Philip Davey & Yaqi Sun & Gregory F. Dykes & Fei Zhou & Tracy Lawson & Peter J. Nixon & Yongjun Lin & Lu-Ning Liu, 2023. "Engineering α-carboxysomes into plant chloroplasts to support autotrophic photosynthesis," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Tao Ni & Qiuyao Jiang & Pei Cing Ng & Juan Shen & Hao Dou & Yanan Zhu & Julika Radecke & Gregory F. Dykes & Fang Huang & Lu-Ning Liu & Peijun Zhang, 2023. "Intrinsically disordered CsoS2 acts as a general molecular thread for α-carboxysome shell assembly," Nature Communications, Nature, vol. 14(1), pages 1-9, December.

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