Molecular principles of the assembly and construction of a carboxysome shell.
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| Auteurs principaux: | , , , , , , , , , , |
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| Format: | Artículo científico |
| Langue: | en |
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Science advances
2024
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| _version_ | 1868266275354968066 |
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| author | Wang, Peng Li, Jianxun Li, Tianpei Li, Kang Ng, Pei Cing Wang, Saimeng Chriscoli, Vincent Basle, Arnaud Marles-Wright, Jon Zhang, Yu-Zhong Liu, Lu-Ning |
| author_facet | Wang, Peng Li, Jianxun Li, Tianpei Li, Kang Ng, Pei Cing Wang, Saimeng Chriscoli, Vincent Basle, Arnaud Marles-Wright, Jon Zhang, Yu-Zhong Liu, Lu-Ning Wang, Peng Li, Jianxun Li, Tianpei Li, Kang Ng, Pei Cing Wang, Saimeng Chriscoli, Vincent Basle, Arnaud Marles-Wright, Jon Zhang, Yu-Zhong Liu, Lu-Ning |
| collection | PubMed - marine biology |
| contents | Molecular principles of the assembly and construction of a carboxysome shell. Wang, Peng Li, Jianxun Li, Tianpei Li, Kang Ng, Pei Cing Wang, Saimeng Chriscoli, Vincent Basle, Arnaud Marles-Wright, Jon Zhang, Yu-Zhong Liu, Lu-Ning Cryoelectron Microscopy Bacterial Proteins Ribulose-Bisphosphate Carboxylase Carbon Dioxide Models, Molecular Protein Multimerization Organelles Intracellular compartmentalization enhances biological reactions, crucial for cellular function and survival. An example is the carboxysome, a bacterial microcompartment for CO fixation. The carboxysome uses a polyhedral protein shell made of hexamers, pentamers, and trimers to encapsulate Rubisco, increasing CO levels near Rubisco to enhance carboxylation. Despite their role in the global carbon cycle, the molecular mechanisms behind carboxysome shell assembly remain unclear. Here, we present a structural characterization of α-carboxysome shells generated from recombinant systems, which contain all shell proteins and the scaffolding protein CsoS2. Atomic-resolution cryo-electron microscopy of the shell assemblies, with a maximal size of 54 nm, unveil diverse assembly interfaces between shell proteins, detailed interactions of CsoS2 with shell proteins to drive shell assembly, and the formation of heterohexamers and heteropentamers by different shell protein paralogs, facilitating the assembly of larger empty shells. Our findings provide mechanistic insights into the construction principles of α-carboxysome shells and the role of CsoS2 in governing α-carboxysome assembly and functionality. |
| format | Artículo científico |
| id | pubmed_39612341 |
| institution | PubMed |
| language | en |
| publishDate | 2024 |
| publisher | Science advances |
| record_format | pubmed |
| spellingShingle | Molecular principles of the assembly and construction of a carboxysome shell. Wang, Peng Li, Jianxun Li, Tianpei Li, Kang Ng, Pei Cing Wang, Saimeng Chriscoli, Vincent Basle, Arnaud Marles-Wright, Jon Zhang, Yu-Zhong Liu, Lu-Ning Cryoelectron Microscopy Bacterial Proteins Ribulose-Bisphosphate Carboxylase Carbon Dioxide Models, Molecular Protein Multimerization Organelles Molecular principles of the assembly and construction of a carboxysome shell. Wang, Peng Li, Jianxun Li, Tianpei Li, Kang Ng, Pei Cing Wang, Saimeng Chriscoli, Vincent Basle, Arnaud Marles-Wright, Jon Zhang, Yu-Zhong Liu, Lu-Ning Cryoelectron Microscopy Bacterial Proteins Ribulose-Bisphosphate Carboxylase Carbon Dioxide Models, Molecular Protein Multimerization Organelles Intracellular compartmentalization enhances biological reactions, crucial for cellular function and survival. An example is the carboxysome, a bacterial microcompartment for CO fixation. The carboxysome uses a polyhedral protein shell made of hexamers, pentamers, and trimers to encapsulate Rubisco, increasing CO levels near Rubisco to enhance carboxylation. Despite their role in the global carbon cycle, the molecular mechanisms behind carboxysome shell assembly remain unclear. Here, we present a structural characterization of α-carboxysome shells generated from recombinant systems, which contain all shell proteins and the scaffolding protein CsoS2. Atomic-resolution cryo-electron microscopy of the shell assemblies, with a maximal size of 54 nm, unveil diverse assembly interfaces between shell proteins, detailed interactions of CsoS2 with shell proteins to drive shell assembly, and the formation of heterohexamers and heteropentamers by different shell protein paralogs, facilitating the assembly of larger empty shells. Our findings provide mechanistic insights into the construction principles of α-carboxysome shells and the role of CsoS2 in governing α-carboxysome assembly and functionality. |
| title | Molecular principles of the assembly and construction of a carboxysome shell. |
| topic | Cryoelectron Microscopy Bacterial Proteins Ribulose-Bisphosphate Carboxylase Carbon Dioxide Models, Molecular Protein Multimerization Organelles |
| url | https://pubmed.ncbi.nlm.nih.gov/39612341/ |