ArticlemBio2024
Uncovering the roles of the scaffolding protein CsoS2 in mediating the assembly and shape of the α-carboxysome shell.
Article in mBio, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- From fundamental understanding to engineering of carboxysomes for biotechnological applications.Plant communications · 2026Review
- Architectural and biochemical advances in understanding microbial COThe Plant journal : for cell and molecular biology · 2026Review
- Recent insights into α-carboxysome structure, mechanism, and assembly.Journal of bacteriology · 2026Review
- Construction of artificial organellesChemical science · 2025Review
- Structure and encapsulation of carbonic anhydrase within the α-carboxysome.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Understanding carboxysomes to enhance carbon fixation in crops.Biochemical Society transactions · 2025Review
- Symmetry-adjusted cryo-EM analysis unveils the detailed linker protein CsoS2 interactions within the α-carboxysome shell.Plant physiology · 2025Article
- Rubisco packaging and stoichiometric composition of the native β-carboxysome in Synechococcus elongatus PCC7942.Plant physiology · 2024Article
- Molecular principles of the assembly and construction of a carboxysome shell.Science advances · 2024Article
- Atomic view of photosynthetic metabolite permeability pathways and confinement in synthetic carboxysome shells.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Rubisco packaging and stoichiometric composition of a native β-carboxysome.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Carboxysomes are proteinaceous organelles featuring icosahedral protein shells that enclose the carbon-fixing enzymes, ribulose-1,5-bisphosphate carboxylase oxygenase (Rubisco), along with carbonic anhydrase. The intrinsically disordered scaffolding protein CsoS2 plays a vital role in the construction of α-carboxysomes through bridging the shell and cargo enzymes. The N-terminal domain of CsoS2 binds Rubisco and facilitates Rubisco packaging within the α-carboxysome, whereas the C-terminal domain of CsoS2 (CsoS2-C) anchors to the shell and promotes shell assembly. However, the role of the middle region of CsoS2 (CsoS2-M) has remained elusive. Here, we conducted in-depth examinations on the function of CsoS2-M in the assembly of the α-carboxysome shell by generating a series of recombinant shell variants in the absence of cargos. Our results reveal that CsoS2-M assists CsoS2-C in the assembly of the α-carboxysome shell and plays an important role in shaping the α-carboxysome shell through enhancing the association of shell proteins on both the facet-facet interfaces and flat shell facets. Moreover, CsoS2-M is responsible for recruiting the C-terminal truncated isoform of CsoS2, CsoS2A, into α-carboxysomes, which is crucial for Rubisco encapsulation and packaging. This study not only deepens our knowledge of how the carboxysome shell is constructed and regulated but also lays the groundwork for engineering and repurposing carboxysome-based nanostructures for diverse biotechnological purposes. IMPORTANCE: Carboxysomes are a paradigm of organelle-like structures in cyanobacteria and many proteobacteria. These nanoscale compartments enclose Rubisco and carbonic anhydrase within an icosahedral virus-like shell to improve CO
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