Structure and assembly of cargo Rubisco in two native α-carboxysomes

Tao Ni, Yaqi Sun, Will Burn, Monsour M. J. Al-Hazeem, Yanan Zhu, Xiulian Yu, Lu-Ning Liu () and Peijun Zhang ()
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Tao Ni: University of Oxford
Yaqi Sun: University of Liverpool
Will Burn: University of Oxford
Monsour M. J. Al-Hazeem: University of Liverpool
Yanan Zhu: University of Oxford
Xiulian Yu: University of Oxford
Lu-Ning Liu: University of Liverpool
Peijun Zhang: University of Oxford

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

Abstract: Abstract Carboxysomes are a family of bacterial microcompartments in cyanobacteria and chemoautotrophs. They encapsulate Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) and carbonic anhydrase catalyzing carbon fixation inside a proteinaceous shell. How Rubisco complexes pack within the carboxysomes is unknown. Using cryo-electron tomography, we determine the distinct 3D organization of Rubisco inside two distant α-carboxysomes from a marine α-cyanobacterium Cyanobium sp. PCC 7001 where Rubiscos are organized in three concentric layers, and from a chemoautotrophic bacterium Halothiobacillus neapolitanus where they form intertwining spirals. We further resolve the structures of native Rubisco as well as its higher-order assembly at near-atomic resolutions by subtomogram averaging. The structures surprisingly reveal that the authentic intrinsically disordered linker protein CsoS2 interacts with Rubiscos in native carboxysomes but functions distinctively in the two α-carboxysomes. In contrast to the uniform Rubisco-CsoS2 association in the Cyanobium α-carboxysome, CsoS2 binds only to the Rubiscos close to the shell in the Halo α-carboxysome. Our findings provide critical knowledge of the assembly principles of α-carboxysomes, which may aid in the rational design and repurposing of carboxysome structures for new functions.

Date: 2022
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DOI: 10.1038/s41467-022-32004-w

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