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Rubisco forms a lattice inside alpha-carboxysomes.

Lauren Ann Metskas1,2,3, Davi Ortega4, Luke M Oltrogge5

  • 1Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, USA. metskas@purdue.edu.

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|August 18, 2022
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Summary
This summary is machine-generated.

Prokaryotic microcompartments like alpha-carboxysomes organize Rubisco enzymes for carbon fixation. Cryo-electron tomography reveals Rubisco polymerization into a lattice, maintaining accessibility within the microcompartment.

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Area of Science:

  • Cellular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Prokaryotic microcompartments are crucial for biological processes but their complex structures remain poorly understood.
  • Structural heterogeneity hinders a complete understanding of microcompartment architecture and function.
  • Alpha-carboxysomes are key microcompartments involved in carbon fixation.

Purpose of the Study:

  • To elucidate the in vivo structure and organization of Rubisco cargo within alpha-carboxysomes.
  • To understand how Rubisco is arranged to optimize carbon fixation efficiency.
  • To investigate the balance between order and disorder in microcompartment protein organization.

Main Methods:

  • Cryo-electron tomography was used to image alpha-carboxysomes at high resolution.
  • Subtomogram averaging was employed to determine the arrangement of Rubisco within the carboxysome.
  • Analysis focused on the spatial organization of Rubisco, CsoSCA, and CsoS2.

Main Results:

  • Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) polymerizes in vivo into fibrils within the alpha-carboxysome, facilitated by its small subunit.
  • These Rubisco fibrils pack into a lattice exhibiting six-fold pseudo-symmetry.
  • This ordered yet flexible arrangement maintains access to Rubisco active sites and binding sites for CsoSCA and CsoS2, even at high protein concentrations (>800 μM).

Conclusions:

  • The study provides a high-resolution structural characterization of Rubisco cargo organization within alpha-carboxysomes.
  • The findings reveal a novel mechanism of enzyme polymerization and lattice formation for efficient carbon fixation.
  • This work offers insights into the principles governing protein organization within biological microcompartments.