Intrinsically disordered CsoS2 acts as a general molecular thread for α-carboxysome shell assembly
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 engineered α-carboxysome shells using minimal shell components and determined 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 uncovered in CsoS2 a remarkable 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-govern carboxysome shell assembly and cargo encapsulation and further advances synthetic engineering of carboxysomes for diverse biotechnological applications..
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Preprint| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
bioRxiv.org - (2024) vom: 23. Apr. Zur Gesamtaufnahme - year:2024 |
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| Sprache: |
Englisch |
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| Beteiligte Personen: |
Ni, Tao [VerfasserIn] |
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| doi: |
10.1101/2023.06.24.546370 |
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| PPN (Katalog-ID): |
XBI039992810 |
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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 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 engineered α-carboxysome shells using minimal shell components and determined 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 uncovered in CsoS2 a remarkable 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-govern carboxysome shell assembly and cargo encapsulation and further advances synthetic engineering of carboxysomes for diverse biotechnological applications. | ||
| 650 | 4 | |a Biology |7 (dpeaa)DE-84 | |
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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 |0 (orcid)0000-0003-1803-691X |4 aut | |
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