Intrinsically disordered CsoS2 acts as a general molecular thread for α-carboxysome shell assembly
© 2023. Springer Nature Limited..
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.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2023 |
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| Erschienen: |
2023 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:14 |
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| Enthalten in: |
Nature communications - 14(2023), 1 vom: 07. Sept., Seite 5512 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Ni, Tao [VerfasserIn] |
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| Links: |
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| Themen: |
EC 4.1.1.39 |
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| Anmerkungen: |
Date Completed 11.09.2023 Date Revised 12.02.2024 published: Electronic Citation Status MEDLINE |
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| doi: |
10.1038/s41467-023-41211-y |
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| funding: |
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| Förderinstitution / Projekttitel: |
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NLM361769180 |
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| 245 | 1 | 0 | |a Intrinsically disordered CsoS2 acts as a general molecular thread for α-carboxysome shell assembly |
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| 520 | |a © 2023. Springer Nature Limited. | ||
| 520 | |a 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 | ||
| 650 | 4 | |a Journal Article | |
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| 700 | 1 | |a Jiang, Qiuyao |e verfasserin |4 aut | |
| 700 | 1 | |a Ng, Pei Cing |e verfasserin |4 aut | |
| 700 | 1 | |a Shen, Juan |e verfasserin |4 aut | |
| 700 | 1 | |a Dou, Hao |e verfasserin |4 aut | |
| 700 | 1 | |a Zhu, Yanan |e verfasserin |4 aut | |
| 700 | 1 | |a Radecke, Julika |e verfasserin |4 aut | |
| 700 | 1 | |a Dykes, Gregory F |e verfasserin |4 aut | |
| 700 | 1 | |a Huang, Fang |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Lu-Ning |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Peijun |e verfasserin |4 aut | |
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