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

Ni, Tao, Sun, Yaqi, Burn, Will, Al-Hazeem, Monsour MJ, Zhu, Yanan, Yu, Xiulian, Liu, Lu-Ning ORCID: 0000-0002-8884-4819 and Zhang, Peijun
(2022) Structure and assembly of cargo Rubisco in two native a-carboxysomes. NATURE COMMUNICATIONS, 13 (1). 4299-.

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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.

Item Type: Article
Uncontrolled Keywords: Organelles, Cyanobacteria, Halothiobacillus, Carbon Dioxide, Ribulose-Bisphosphate Carboxylase, Bacterial Proteins, Carbon Cycle, Intrinsically Disordered Proteins
Divisions: Faculty of Health and Life Sciences
Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology
Depositing User: Symplectic Admin
Date Deposited: 26 Jul 2022 08:39
Last Modified: 17 Aug 2023 07:51
DOI: 10.1038/s41467-022-32004-w
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