Ni, Tao, Jiang, qiuyao, Ng, PEI CING 
ORCID: 0000-0003-0905-0584, Shen, Juan, Dou, Hao, Zhu, Yanan, Radecke, Julika, Dykes, Gregory ORCID: 0000-0002-0626-9487, Huang, Fang, Liu, Luning ORCID: 0000-0002-8884-4819 et al (show 1 more authors)
(2023)
Intrinsically disordered CsoS2 acts as a general molecular thread for α-carboxysome shell assembly.
Nature Communications, 14 (1).
5512-.
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Abstract
Carboxysomes are a paradigm of self-assembling proteinaceous organelles found in nature, offering compartmentalisation of enzymes and pathways to enhance carbon fixation. In α-carboxysomes, the disordered linker protein CsoS2 plays an essential role in carboxysome assembly and Rubisco encapsulation. Its mechanism of action, however, is not fully understood. Here we synthetically engineer α-carboxysome shells using minimal shell components and determine cryoEM structures of these to decipher the principle of shell assembly and encapsulation. The structures reveal that the intrinsically disordered CsoS2 C-terminus is well-structured and acts as a universal "molecular thread" stitching through multiple shell protein interfaces. We further uncover in CsoS2 a highly conserved repetitive key interaction motif, [IV]TG, which is critical to the shell assembly and architecture. Our study provides a general mechanism for the CsoS2-governed carboxysome shell assembly and cargo encapsulation and further advances synthetic engineering of carboxysomes for diverse biotechnological applications.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Ribulose-Bisphosphate Carboxylase, Cryoelectron Microscopy, Biotechnology, Engineering, Software |
| 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: | 11 Sep 2023 08:06 |
| Last Modified: | 25 Oct 2023 16:55 |
| DOI: | 10.1038/s41467-023-41211-y |
| Related URLs: | |
| URI: | https://livrepository.liverpool.ac.uk/id/eprint/3172648 |
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