Rubisco forms a lattice inside alpha-carboxysomes

Lauren Ann Metskas (), Davi Ortega, Luke M. Oltrogge, Cecilia Blikstad, Derik R. Lovejoy, Thomas G. Laughlin, David F. Savage and Grant J. Jensen ()
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Lauren Ann Metskas: California Institute of Technology
Davi Ortega: California Institute of Technology
Luke M. Oltrogge: University of California
Cecilia Blikstad: University of California
Derik R. Lovejoy: Purdue University
Thomas G. Laughlin: University of California
David F. Savage: University of California
Grant J. Jensen: California Institute of Technology

Nature Communications, 2022, vol. 13, issue 1, 1-9

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-32584-7

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